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Title: 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