The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1211-7, 2010 Oct 01.
Article
de En
| MEDLINE
| ID: mdl-20944213
ABSTRACT
The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded ß-sheet wrapped around a single α-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell-wall stress or host-pathogen interactions.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Pseudomonas aeruginosa
/
Protéines bactériennes
/
Glycolipides
/
Pliage des protéines
Type d'étude:
Prognostic_studies
Langue:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Année:
2010
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique