Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism

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Abstract

The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+Β fold comprising two Β-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.

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Bakolitsa, C., Kumar, A., Carlton, D., Miller, M. D., Krishna, S. S., Abdubek, P., … Wilson, I. A. (2010). Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(10), 1205–1210. https://doi.org/10.1107/S1744309109023689

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