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[摘要]：The crystal structure for cce_0566 (171 aa, 19.4 kDa), a DUF269 annotated protein from the diazotrophic cyanobacterium Cyanothece sp. ATCC 51142, was determined to 1.60 angstrom resolution. Cce_0566 is a homodimer with each molecule composed of eight alpha-helices folded on one side of a three strand anti-parallel beta-sheet. Hydrophobic interactions between the side chains of largely conserved residues on the surface of each beta-sheet hold the dimer together. The fold observed for cce_0566 may be unique to proteins in the DUF269 family, hence, the protein may also have a function unique to nitrogen fixation. A solvent accessible cleft containing conserved charged residues near the dimer interface could represent the active site or ligand-binding surface for the protein's biological function. Structured summary of protein interactions: DUF269 and DUF269 bind by x-ray crystallography (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. |
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