Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
Journal Article
·
· Acta Crystallogr. F
The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel {alpha} + {beta} fold comprising two {beta}-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.
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- NIGMS
- OSTI ID:
- 1022277
- Journal Information:
- Acta Crystallogr. F, Vol. 66, Issue (10) ; 10, 2010; ISSN 1744-3091
- Country of Publication:
- United States
- Language:
- ENGLISH
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