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dc.contributor.author
Jack, Benjamin R.
dc.contributor.author
Meyer, Austin G.
dc.contributor.author
Echave, Julián
dc.contributor.author
Wilke, Claus O.
dc.date.available
2018-05-11T21:26:11Z
dc.date.issued
2016-05
dc.identifier.citation
Jack, Benjamin R.; Meyer, Austin G.; Echave, Julián; Wilke, Claus O.; Functional Sites Induce Long-Range Evolutionary Constraints in Enzymes; Public Library of Science; PLoS Biology; 14; 5; 5-2016; 1-23; e1002452
dc.identifier.uri
http://hdl.handle.net/11336/45007
dc.description.abstract
Functional residues in proteins tend to be highly conserved over evolutionary time. However, to what extent functional sites impose evolutionary constraints on nearby or even more distant residues is not known. Here, we report pervasive conservation gradients toward catalytic residues in a dataset of 524 distinct enzymes: evolutionary conservation decreases approximately linearly with increasing distance to the nearest catalytic residue in the protein structure. This trend encompasses, on average, 80% of the residues in any enzyme, and it is independent of known structural constraints on protein evolution such as residue packing or solvent accessibility. Further, the trend exists in both monomeric and multimeric enzymes and irrespective of enzyme size and/or location of the active site in the enzyme structure. By contrast, sites in protein–protein interfaces, unlike catalytic residues, are only weakly conserved and induce only minor rate gradients. In aggregate, these observations show that functional sites, and in particular catalytic residues, induce long-range evolutionary constraints in enzymes.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Public Library of Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Protein
dc.subject
Evolution
dc.subject
Functional
dc.subject
Constraints
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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Otras Ciencias Químicas
dc.subject.classification
Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Functional Sites Induce Long-Range Evolutionary Constraints in Enzymes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-05-11T20:38:19Z
dc.identifier.eissn
1545-7885
dc.journal.volume
14
dc.journal.number
5
dc.journal.pagination
1-23; e1002452
dc.journal.pais
Estados Unidos
dc.journal.ciudad
San Francisco
dc.description.fil
Fil: Jack, Benjamin R.. University of Texas at Austin; Estados Unidos
dc.description.fil
Fil: Meyer, Austin G.. University of Texas at Austin; Estados Unidos
dc.description.fil
Fil: Echave, Julián. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Wilke, Claus O.. University of Texas at Austin; Estados Unidos
dc.journal.title
PLoS Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1371/journal.pbio.1002452
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.1002452
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