Mostrar el registro sencillo del ítem

dc.contributor.author
Parisi, Gustavo Daniel
dc.contributor.author
Fornasari, Maria Silvina
dc.contributor.author
Echave, Julián
dc.date.available
2019-03-14T14:50:17Z
dc.date.issued
2000-12
dc.identifier.citation
Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Echave, Julián; Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins; Academic Press Inc Elsevier Science; Molecular Phylogenetics and Evolution; 14; 3; 12-2000; 323-334
dc.identifier.issn
1055-7903
dc.identifier.uri
http://hdl.handle.net/11336/71608
dc.description.abstract
We studied the evolutionary relationships between γ-carbonic anhydrase (γ-CA) and a very diverse group of proteins that share the sequence motif characteristic of the left-handed parallel β-helix (LβH) fold. This sequence motif is characterized by the imperfect tandem repetition of short hexapeptide units, which makes it difficult to obtain a reliable alignment based on sequence information alone. To solve this problem, we used a structural alignment of three members of the group with known crystallographic structures as a seed to obtain a reliable sequence alignment. Then, we applied protein maximum-parsimony and maximum-likelihood phylogenetic inference methods to this alignment. We found that γ-CA belongs to a diverse superfamily of proteins that share the LβH domain. This superfamily is composed mainly of acyltransferases. The most remarkable feature of the phylogenetic tree obtained is that its main branches group together functionally related proteins, so that the coarse topology can be rather easily explained in terms of functional diversification. Regarding the main branch of the tree containing γ-CA, we found that, in addition to the group of its closest relatives that had already been studied, γ-CA is closely related to the tetrahydrodipicolinate N-succinyltransferases. (C) 2000 Academic Press.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Academic Press Inc Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Protein Evolution
dc.subject
Gamma Carbonic Anhydrase
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-03-14T14:21:58Z
dc.journal.volume
14
dc.journal.number
3
dc.journal.pagination
323-334
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
dc.description.fil
Fil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
dc.description.fil
Fil: Echave, Julián. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
Molecular Phylogenetics and Evolution
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1006/mpev.1999.0734
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1055790399907340


Archivos asociados

Documento no disponible

Comunidades y colecciones

Mostrar el registro sencillo del ítem