Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1205-10, 2010 Oct 01.
Article
de En
| MEDLINE
| ID: mdl-20944212
ABSTRACT
The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+ß fold comprising two ß-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokaryotic S-adenosylmethionine decarboxylases, is consistent with a role in amino-acid metabolism. Genomic neighborhood analysis of LP2179 supports this functional assignment, which might also then be extended to PF08868 and PF08968.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Protéines bactériennes
/
Pliage des protéines
/
Lactobacillus plantarum
/
Acides aminés
Langue:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Année:
2010
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique