Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues

Detalhes bibliográficos
Autor(a) principal: Rigden, Daniel John
Data de Publicação: 2002
Outros Autores: Franco, Octávio Luiz
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UCB
Texto Completo: http://twingo.ucb.br:8080/jspui/handle/10869/669
https://repositorio.ucb.br:9443/jspui/handle/123456789/7880
Resumo: Abstract X-ray crystallography and bioinformatics studies reveal a tendency for the right-handed L-helix domain architecture to be associated with carbohydrate binding proteins. Here we demonstrate the presence of catalytic L-helix domains in glycoside hydrolase (GH) families 49, 55 and 87 and provide evidence for their sharing a common evolutionary ancestor with two structurally characterized GH families, numbers 28 and 82. This domain assignment helps assign catalytic residues to each family. Further analysis of domain architecture reveals the association of carbohydrate binding modules with catalytic GH L-helices, as well as an unexpected pair of L-helix domains in GH family 55. ) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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spelling Rigden, Daniel JohnFranco, Octávio Luiz2016-10-10T03:52:58Z2016-10-10T03:52:58Z2002RIGDEN, Daniel John; FRANCO, Octávio Luiz. Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87: Domain architecture, modelling and assignment of catalytic residues. FEBS Letters, v. 530, p. 225-232, 2002.http://twingo.ucb.br:8080/jspui/handle/10869/669https://repositorio.ucb.br:9443/jspui/handle/123456789/7880Abstract X-ray crystallography and bioinformatics studies reveal a tendency for the right-handed L-helix domain architecture to be associated with carbohydrate binding proteins. Here we demonstrate the presence of catalytic L-helix domains in glycoside hydrolase (GH) families 49, 55 and 87 and provide evidence for their sharing a common evolutionary ancestor with two structurally characterized GH families, numbers 28 and 82. This domain assignment helps assign catalytic residues to each family. Further analysis of domain architecture reveals the association of carbohydrate binding modules with catalytic GH L-helices, as well as an unexpected pair of L-helix domains in GH family 55. ) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.Made available in DSpace on 2016-10-10T03:52:58Z (GMT). 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dc.title.pt_BR.fl_str_mv Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
title Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
spellingShingle Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
Rigden, Daniel John
Glycosidase
Iterative database search
Fold recognition
Evolutionary relationship
title_short Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
title_full Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
title_fullStr Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
title_full_unstemmed Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
title_sort Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87:domain architecture, modelling and assignment of catalytic residues
author Rigden, Daniel John
author_facet Rigden, Daniel John
Franco, Octávio Luiz
author_role author
author2 Franco, Octávio Luiz
author2_role author
dc.contributor.author.fl_str_mv Rigden, Daniel John
Franco, Octávio Luiz
dc.subject.por.fl_str_mv Glycosidase
Iterative database search
Fold recognition
Evolutionary relationship
topic Glycosidase
Iterative database search
Fold recognition
Evolutionary relationship
dc.description.abstract.por.fl_txt_mv Abstract X-ray crystallography and bioinformatics studies reveal a tendency for the right-handed L-helix domain architecture to be associated with carbohydrate binding proteins. Here we demonstrate the presence of catalytic L-helix domains in glycoside hydrolase (GH) families 49, 55 and 87 and provide evidence for their sharing a common evolutionary ancestor with two structurally characterized GH families, numbers 28 and 82. This domain assignment helps assign catalytic residues to each family. Further analysis of domain architecture reveals the association of carbohydrate binding modules with catalytic GH L-helices, as well as an unexpected pair of L-helix domains in GH family 55. ) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
dc.description.status.pt_BR.fl_txt_mv Publicado
description Abstract X-ray crystallography and bioinformatics studies reveal a tendency for the right-handed L-helix domain architecture to be associated with carbohydrate binding proteins. Here we demonstrate the presence of catalytic L-helix domains in glycoside hydrolase (GH) families 49, 55 and 87 and provide evidence for their sharing a common evolutionary ancestor with two structurally characterized GH families, numbers 28 and 82. This domain assignment helps assign catalytic residues to each family. Further analysis of domain architecture reveals the association of carbohydrate binding modules with catalytic GH L-helices, as well as an unexpected pair of L-helix domains in GH family 55. ) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
publishDate 2002
dc.date.issued.fl_str_mv 2002
dc.date.accessioned.fl_str_mv 2016-10-10T03:52:58Z
dc.date.available.fl_str_mv 2016-10-10T03:52:58Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
status_str publishedVersion
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dc.identifier.citation.fl_str_mv RIGDEN, Daniel John; FRANCO, Octávio Luiz. Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87: Domain architecture, modelling and assignment of catalytic residues. FEBS Letters, v. 530, p. 225-232, 2002.
dc.identifier.uri.fl_str_mv http://twingo.ucb.br:8080/jspui/handle/10869/669
https://repositorio.ucb.br:9443/jspui/handle/123456789/7880
identifier_str_mv RIGDEN, Daniel John; FRANCO, Octávio Luiz. Beta-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87: Domain architecture, modelling and assignment of catalytic residues. FEBS Letters, v. 530, p. 225-232, 2002.
url http://twingo.ucb.br:8080/jspui/handle/10869/669
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