3nj2 | pdb_00003nj2

Crystal structure of cce_0566 from the cyanobacterium Cyanothece 51142, a protein associated with nitrogen fixation from the DUF269 family

spinqualitylabelsall models 3nj2, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nj2 is a 2 chain structure with sequence from Crocosphaera subtropica ATCC 51142. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.59Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B1WPD5_CROS5 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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