3NJ2
Crystal structure of cce_0566 from the cyanobacterium Cyanothece 51142, a protein associated with nitrogen fixation from the DUF269 family
Summary for 3NJ2
Entry DOI | 10.2210/pdb3nj2/pdb |
Descriptor | DUF269-containing protein (2 entities in total) |
Functional Keywords | cyanobacteria, circadium rhythms, nitrogen fixation, unknown function |
Biological source | Cyanothece sp. ATCC 51142 |
Total number of polymer chains | 2 |
Total formula weight | 39459.21 |
Authors | Robinson, H.,Ralston, C.Y.,Addlagatta, A.,Buchko, G.W. (deposition date: 2010-06-16, release date: 2010-07-07, Last modification date: 2023-09-06) |
Primary citation | Buchko, G.W.,Robinson, H. Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family. Febs Lett., 586:350-355, 2012 Cited by PubMed Abstract: 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 1.60Å resolution. Cce_0566 is a homodimer with each molecule composed of eight α-helices folded on one side of a three strand anti-parallel β-sheet. Hydrophobic interactions between the side chains of largely conserved residues on the surface of each β-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. PubMed: 22289180DOI: 10.1016/j.febslet.2012.01.037 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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