Mapping the distribution of conformational information throughout a protein sequence

Autores
Gebhard, Leopoldo German; Risso, Valeria Alejandra; Santos, Javier; Ferreyra, Raul Gabriel; Noguera, Martín Ezequiel; Ermacora, Mario Roberto
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The three-dimensional structure of protein is encoded in the sequence, but many amino acid residues carry no essential conformational information, and the identity of those that are structure-determining is elusive. By circular permutation and terminal deletion, we produced and purified 25 Bacillus licheniformis β-lactamase (ESBL) variants that lack 5–21 contiguous residues each, and collectively have 82% of the sequence and 92% of the non-local atom–atom contacts eliminated. Circular dichroism and size-exclusion chromatography showed that most of the variants form conformationally heterogeneous mixtures, but by measuring catalytic constants, we found that all populate, to a greater or lesser extent, conformations with the essential features of the native fold. This suggests that no segment of the ESBL sequence is essential to the structure as a whole, which is congruent with the notion that local information and modular organization can impart most of the tertiary fold specificity and cooperativity.
Fil: Gebhard, Leopoldo German. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Risso, Valeria Alejandra. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Santos, Javier. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ferreyra, Raul Gabriel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Noguera, Martín Ezequiel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Protein Folding
Beta-Lactamase
Conformational Information
Sequence Patterns
Folding Code
Folding Units
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:11336/31748
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Mapping the distribution of conformational information throughout a protein sequenceGebhard, Leopoldo GermanRisso, Valeria AlejandraSantos, JavierFerreyra, Raul GabrielNoguera, Martín EzequielErmacora, Mario RobertoProtein FoldingBeta-LactamaseConformational InformationSequence PatternsFolding CodeFolding Unitshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The three-dimensional structure of protein is encoded in the sequence, but many amino acid residues carry no essential conformational information, and the identity of those that are structure-determining is elusive. By circular permutation and terminal deletion, we produced and purified 25 Bacillus licheniformis β-lactamase (ESBL) variants that lack 5–21 contiguous residues each, and collectively have 82% of the sequence and 92% of the non-local atom–atom contacts eliminated. Circular dichroism and size-exclusion chromatography showed that most of the variants form conformationally heterogeneous mixtures, but by measuring catalytic constants, we found that all populate, to a greater or lesser extent, conformations with the essential features of the native fold. This suggests that no segment of the ESBL sequence is essential to the structure as a whole, which is congruent with the notion that local information and modular organization can impart most of the tertiary fold specificity and cooperativity.Fil: Gebhard, Leopoldo German. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Risso, Valeria Alejandra. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Santos, Javier. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Ferreyra, Raul Gabriel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Noguera, Martín Ezequiel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2006-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31748Ermacora, Mario Roberto; Noguera, Martín Ezequiel; Ferreyra, Raul Gabriel; Santos, Javier; Risso, Valeria Alejandra; Gebhard, Leopoldo German; et al.; Mapping the distribution of conformational information throughout a protein sequence; Elsevier; Journal Of Molecular Biology; 358; 1; 2-2006; 280-2880022-2836CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022283606001495info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2006.01.095info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:46:52Zoai:ri.conicet.gov.ar:11336/31748instacron: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:34982025-09-29 09:46:52.34CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Mapping the distribution of conformational information throughout a protein sequence
title Mapping the distribution of conformational information throughout a protein sequence
spellingShingle Mapping the distribution of conformational information throughout a protein sequence
Gebhard, Leopoldo German
Protein Folding
Beta-Lactamase
Conformational Information
Sequence Patterns
Folding Code
Folding Units
title_short Mapping the distribution of conformational information throughout a protein sequence
title_full Mapping the distribution of conformational information throughout a protein sequence
title_fullStr Mapping the distribution of conformational information throughout a protein sequence
title_full_unstemmed Mapping the distribution of conformational information throughout a protein sequence
title_sort Mapping the distribution of conformational information throughout a protein sequence
dc.creator.none.fl_str_mv Gebhard, Leopoldo German
Risso, Valeria Alejandra
Santos, Javier
Ferreyra, Raul Gabriel
Noguera, Martín Ezequiel
Ermacora, Mario Roberto
author Gebhard, Leopoldo German
author_facet Gebhard, Leopoldo German
Risso, Valeria Alejandra
Santos, Javier
Ferreyra, Raul Gabriel
Noguera, Martín Ezequiel
Ermacora, Mario Roberto
author_role author
author2 Risso, Valeria Alejandra
Santos, Javier
Ferreyra, Raul Gabriel
Noguera, Martín Ezequiel
Ermacora, Mario Roberto
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Protein Folding
Beta-Lactamase
Conformational Information
Sequence Patterns
Folding Code
Folding Units
topic Protein Folding
Beta-Lactamase
Conformational Information
Sequence Patterns
Folding Code
Folding Units
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The three-dimensional structure of protein is encoded in the sequence, but many amino acid residues carry no essential conformational information, and the identity of those that are structure-determining is elusive. By circular permutation and terminal deletion, we produced and purified 25 Bacillus licheniformis β-lactamase (ESBL) variants that lack 5–21 contiguous residues each, and collectively have 82% of the sequence and 92% of the non-local atom–atom contacts eliminated. Circular dichroism and size-exclusion chromatography showed that most of the variants form conformationally heterogeneous mixtures, but by measuring catalytic constants, we found that all populate, to a greater or lesser extent, conformations with the essential features of the native fold. This suggests that no segment of the ESBL sequence is essential to the structure as a whole, which is congruent with the notion that local information and modular organization can impart most of the tertiary fold specificity and cooperativity.
Fil: Gebhard, Leopoldo German. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Risso, Valeria Alejandra. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Santos, Javier. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ferreyra, Raul Gabriel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Noguera, Martín Ezequiel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The three-dimensional structure of protein is encoded in the sequence, but many amino acid residues carry no essential conformational information, and the identity of those that are structure-determining is elusive. By circular permutation and terminal deletion, we produced and purified 25 Bacillus licheniformis β-lactamase (ESBL) variants that lack 5–21 contiguous residues each, and collectively have 82% of the sequence and 92% of the non-local atom–atom contacts eliminated. Circular dichroism and size-exclusion chromatography showed that most of the variants form conformationally heterogeneous mixtures, but by measuring catalytic constants, we found that all populate, to a greater or lesser extent, conformations with the essential features of the native fold. This suggests that no segment of the ESBL sequence is essential to the structure as a whole, which is congruent with the notion that local information and modular organization can impart most of the tertiary fold specificity and cooperativity.
publishDate 2006
dc.date.none.fl_str_mv 2006-02
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/11336/31748
Ermacora, Mario Roberto; Noguera, Martín Ezequiel; Ferreyra, Raul Gabriel; Santos, Javier; Risso, Valeria Alejandra; Gebhard, Leopoldo German; et al.; Mapping the distribution of conformational information throughout a protein sequence; Elsevier; Journal Of Molecular Biology; 358; 1; 2-2006; 280-288
0022-2836
CONICET Digital
CONICET
url http://hdl.handle.net/11336/31748
identifier_str_mv Ermacora, Mario Roberto; Noguera, Martín Ezequiel; Ferreyra, Raul Gabriel; Santos, Javier; Risso, Valeria Alejandra; Gebhard, Leopoldo German; et al.; Mapping the distribution of conformational information throughout a protein sequence; Elsevier; Journal Of Molecular Biology; 358; 1; 2-2006; 280-288
0022-2836
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022283606001495
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2006.01.095
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
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.070432

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