The structure, molecular dynamics, and energetics of centrin-melittin complex

Autores
Sosa, Liliana del Valle; Alfaro, Elisa Raquel; Santiago, Jorge Fernando; Narváez, Daniel; Rosado, Marie Cely; Rodríguez, Aslin; Gómez, Ana María; Schreiter, Eric R.; Pastrana Ríos, Belinda
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Centrin is a calcium binding protein (CaBP) belonging to the EF-hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study Chlamydomonas reinhardtii centrin (Crcen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin-MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define Crcen-MLT complex formation. Two-dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I', I'*, and side chain bands for 13C-Crcen, MLT, and the 13C-Crcen-MLT complex. This approach resulted in the determination of MLT's increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin-MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP-MLT complex by X-ray crystallography, which shows that MLT has a different binding orientation than previously characterized centrin-bound peptides. Finally, all of the experimental results presented herein are consistent with centrin maintaining an extended conformation while interacting with MLT. The molecular implications of these results are: (1) the recognition of hydrophobic contacts as requirements for initial binding, (2) minimum electrostatic interactions within the C-terminal end of the peptide, and (3) van der Waals interactions within MLTs N-terminal end are required for complex formation.
Fil: Sosa, Liliana del Valle. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; Argentina
Fil: Alfaro, Elisa Raquel. Universidad de Puerto Rico; Puerto Rico
Fil: Santiago, Jorge Fernando. Universidad de Puerto Rico; Puerto Rico
Fil: Narváez, Daniel. Universidad de Puerto Rico; Puerto Rico
Fil: Rosado, Marie Cely. Universidad de Puerto Rico; Puerto Rico
Fil: Rodríguez, Aslin. Universidad de Puerto Rico; Puerto Rico
Fil: Gómez, Ana María. Universidad de Puerto Rico; Puerto Rico
Fil: Schreiter, Eric R.. Universidad de Puerto Rico; Puerto Rico
Fil: Pastrana Ríos, Belinda. Universidad de Puerto Rico; Puerto Rico
Materia
2D IR CORRELATION
CALCIUM BINDING PROTEIN
CENTRIN
COMPLEX DISSOCIATION
COMPLEX FORMATION
ISOTHERMAL TITRATION CALORIMETRY
MELITTIN
PROTEIN-PROTEIN INTERACTION
SPECTROSCOPY
UNFOLDING
X-RAY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/193473
Acceder
id CONICETDig_6469eeb2c96c54b678f954632ccc6f34
oai_identifier_str oai:ri.conicet.gov.ar:11336/193473
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The structure, molecular dynamics, and energetics of centrin-melittin complexSosa, Liliana del ValleAlfaro, Elisa RaquelSantiago, Jorge FernandoNarváez, DanielRosado, Marie CelyRodríguez, AslinGómez, Ana MaríaSchreiter, Eric R.Pastrana Ríos, Belinda2D IR CORRELATIONCALCIUM BINDING PROTEINCENTRINCOMPLEX DISSOCIATIONCOMPLEX FORMATIONISOTHERMAL TITRATION CALORIMETRYMELITTINPROTEIN-PROTEIN INTERACTIONSPECTROSCOPYUNFOLDINGX-RAYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Centrin is a calcium binding protein (CaBP) belonging to the EF-hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study Chlamydomonas reinhardtii centrin (Crcen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin-MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define Crcen-MLT complex formation. Two-dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I', I'*, and side chain bands for 13C-Crcen, MLT, and the 13C-Crcen-MLT complex. This approach resulted in the determination of MLT's increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin-MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP-MLT complex by X-ray crystallography, which shows that MLT has a different binding orientation than previously characterized centrin-bound peptides. Finally, all of the experimental results presented herein are consistent with centrin maintaining an extended conformation while interacting with MLT. The molecular implications of these results are: (1) the recognition of hydrophobic contacts as requirements for initial binding, (2) minimum electrostatic interactions within the C-terminal end of the peptide, and (3) van der Waals interactions within MLTs N-terminal end are required for complex formation.Fil: Sosa, Liliana del Valle. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; ArgentinaFil: Alfaro, Elisa Raquel. Universidad de Puerto Rico; Puerto RicoFil: Santiago, Jorge Fernando. Universidad de Puerto Rico; Puerto RicoFil: Narváez, Daniel. Universidad de Puerto Rico; Puerto RicoFil: Rosado, Marie Cely. Universidad de Puerto Rico; Puerto RicoFil: Rodríguez, Aslin. Universidad de Puerto Rico; Puerto RicoFil: Gómez, Ana María. Universidad de Puerto Rico; Puerto RicoFil: Schreiter, Eric R.. Universidad de Puerto Rico; Puerto RicoFil: Pastrana Ríos, Belinda. Universidad de Puerto Rico; Puerto RicoWiley-liss, div John Wiley & Sons Inc.2011-08-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/193473Sosa, Liliana del Valle; Alfaro, Elisa Raquel; Santiago, Jorge Fernando; Narváez, Daniel; Rosado, Marie Cely; et al.; The structure, molecular dynamics, and energetics of centrin-melittin complex; Wiley-liss, div John Wiley & Sons Inc.; Proteins: Structure, Function And Genetics; 79; 11; 2-8-2011; 3132-31430887-35851097-0134CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/prot.23142info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1002/prot.23142info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:22:39Zoai:ri.conicet.gov.ar:11336/193473instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:22:39.392CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The structure, molecular dynamics, and energetics of centrin-melittin complex
title The structure, molecular dynamics, and energetics of centrin-melittin complex
spellingShingle The structure, molecular dynamics, and energetics of centrin-melittin complex
Sosa, Liliana del Valle
2D IR CORRELATION
CALCIUM BINDING PROTEIN
CENTRIN
COMPLEX DISSOCIATION
COMPLEX FORMATION
ISOTHERMAL TITRATION CALORIMETRY
MELITTIN
PROTEIN-PROTEIN INTERACTION
SPECTROSCOPY
UNFOLDING
X-RAY
title_short The structure, molecular dynamics, and energetics of centrin-melittin complex
title_full The structure, molecular dynamics, and energetics of centrin-melittin complex
title_fullStr The structure, molecular dynamics, and energetics of centrin-melittin complex
title_full_unstemmed The structure, molecular dynamics, and energetics of centrin-melittin complex
title_sort The structure, molecular dynamics, and energetics of centrin-melittin complex
dc.creator.none.fl_str_mv Sosa, Liliana del Valle
Alfaro, Elisa Raquel
Santiago, Jorge Fernando
Narváez, Daniel
Rosado, Marie Cely
Rodríguez, Aslin
Gómez, Ana María
Schreiter, Eric R.
Pastrana Ríos, Belinda
author Sosa, Liliana del Valle
author_facet Sosa, Liliana del Valle
Alfaro, Elisa Raquel
Santiago, Jorge Fernando
Narváez, Daniel
Rosado, Marie Cely
Rodríguez, Aslin
Gómez, Ana María
Schreiter, Eric R.
Pastrana Ríos, Belinda
author_role author
author2 Alfaro, Elisa Raquel
Santiago, Jorge Fernando
Narváez, Daniel
Rosado, Marie Cely
Rodríguez, Aslin
Gómez, Ana María
Schreiter, Eric R.
Pastrana Ríos, Belinda
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv 2D IR CORRELATION
CALCIUM BINDING PROTEIN
CENTRIN
COMPLEX DISSOCIATION
COMPLEX FORMATION
ISOTHERMAL TITRATION CALORIMETRY
MELITTIN
PROTEIN-PROTEIN INTERACTION
SPECTROSCOPY
UNFOLDING
X-RAY
topic 2D IR CORRELATION
CALCIUM BINDING PROTEIN
CENTRIN
COMPLEX DISSOCIATION
COMPLEX FORMATION
ISOTHERMAL TITRATION CALORIMETRY
MELITTIN
PROTEIN-PROTEIN INTERACTION
SPECTROSCOPY
UNFOLDING
X-RAY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Centrin is a calcium binding protein (CaBP) belonging to the EF-hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study Chlamydomonas reinhardtii centrin (Crcen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin-MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define Crcen-MLT complex formation. Two-dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I', I'*, and side chain bands for 13C-Crcen, MLT, and the 13C-Crcen-MLT complex. This approach resulted in the determination of MLT's increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin-MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP-MLT complex by X-ray crystallography, which shows that MLT has a different binding orientation than previously characterized centrin-bound peptides. Finally, all of the experimental results presented herein are consistent with centrin maintaining an extended conformation while interacting with MLT. The molecular implications of these results are: (1) the recognition of hydrophobic contacts as requirements for initial binding, (2) minimum electrostatic interactions within the C-terminal end of the peptide, and (3) van der Waals interactions within MLTs N-terminal end are required for complex formation.
Fil: Sosa, Liliana del Valle. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; Argentina
Fil: Alfaro, Elisa Raquel. Universidad de Puerto Rico; Puerto Rico
Fil: Santiago, Jorge Fernando. Universidad de Puerto Rico; Puerto Rico
Fil: Narváez, Daniel. Universidad de Puerto Rico; Puerto Rico
Fil: Rosado, Marie Cely. Universidad de Puerto Rico; Puerto Rico
Fil: Rodríguez, Aslin. Universidad de Puerto Rico; Puerto Rico
Fil: Gómez, Ana María. Universidad de Puerto Rico; Puerto Rico
Fil: Schreiter, Eric R.. Universidad de Puerto Rico; Puerto Rico
Fil: Pastrana Ríos, Belinda. Universidad de Puerto Rico; Puerto Rico
description Centrin is a calcium binding protein (CaBP) belonging to the EF-hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study Chlamydomonas reinhardtii centrin (Crcen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin-MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define Crcen-MLT complex formation. Two-dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I', I'*, and side chain bands for 13C-Crcen, MLT, and the 13C-Crcen-MLT complex. This approach resulted in the determination of MLT's increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin-MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP-MLT complex by X-ray crystallography, which shows that MLT has a different binding orientation than previously characterized centrin-bound peptides. Finally, all of the experimental results presented herein are consistent with centrin maintaining an extended conformation while interacting with MLT. The molecular implications of these results are: (1) the recognition of hydrophobic contacts as requirements for initial binding, (2) minimum electrostatic interactions within the C-terminal end of the peptide, and (3) van der Waals interactions within MLTs N-terminal end are required for complex formation.
publishDate 2011
dc.date.none.fl_str_mv 2011-08-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/193473
Sosa, Liliana del Valle; Alfaro, Elisa Raquel; Santiago, Jorge Fernando; Narváez, Daniel; Rosado, Marie Cely; et al.; The structure, molecular dynamics, and energetics of centrin-melittin complex; Wiley-liss, div John Wiley & Sons Inc.; Proteins: Structure, Function And Genetics; 79; 11; 2-8-2011; 3132-3143
0887-3585
1097-0134
CONICET Digital
CONICET
url http://hdl.handle.net/11336/193473
identifier_str_mv Sosa, Liliana del Valle; Alfaro, Elisa Raquel; Santiago, Jorge Fernando; Narváez, Daniel; Rosado, Marie Cely; et al.; The structure, molecular dynamics, and energetics of centrin-melittin complex; Wiley-liss, div John Wiley & Sons Inc.; Proteins: Structure, Function And Genetics; 79; 11; 2-8-2011; 3132-3143
0887-3585
1097-0134
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/prot.23142
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1002/prot.23142
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley-liss, div John Wiley & Sons Inc.
publisher.none.fl_str_mv Wiley-liss, div John Wiley & Sons Inc.
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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