The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1160-6, 2010 Oct 01.
Article
em En
| MEDLINE
| ID: mdl-20944206
ABSTRACT
SSO2064 is the first structural representative of PF01796 (DUF35), a large prokaryotic family with a wide phylogenetic distribution. The structure reveals a novel two-domain architecture comprising an N-terminal, rubredoxin-like, zinc ribbon and a C-terminal, oligonucleotide/oligosaccharide-binding (OB) fold domain. Additional N-terminal helical segments may be involved in protein-protein interactions. Domain architectures, genomic context analysis and functional evidence from certain bacterial representatives of this family suggest that these proteins form a novel fatty-acid-binding component that is involved in the biosynthesis of lipids and polyketide antibiotics and that they possibly function as acyl-CoA-binding proteins. This structure has led to a re-evaluation of the DUF35 family, which has now been split into two entries in the latest Pfam release (v.24.0).
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Zinco
/
Acil Coenzima A
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Dobramento de Proteína
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Proteínas Arqueais
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Sulfolobus solfataricus
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2010
Tipo de documento:
Article
País de afiliação:
Estados Unidos