3nj2

Publication Abstract from PubMed

The crystal structure for cce_0566 (171 aa, 19.4kDa), a DUF269 annotated protein from the diazotrophic cyanobacterium Cyanothece sp. ATCC 51142, was determined to 1.60A 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 DUF269bind by x-ray crystallography (View interaction).

Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family.,Buchko GW, Robinson H FEBS Lett. 2012 Feb 17;586(4):350-5. Epub 2012 Jan 28. PMID:22289180^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.