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. 2010 Oct 1;66(Pt 10):1205-10. doi: 10.1107/S1744309109023689. Epub 2009 Oct 27.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / metabolism*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Lactobacillus plantarum / chemistry*
  • Lactobacillus plantarum / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Folding*
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Structural Homology, Protein

Substances

  • Amino Acids
  • Bacterial Proteins

Associated data

  • PDB/2IAY