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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 DOI10.2210/pdb3nj2/pdb
DescriptorDUF269-containing protein (2 entities in total)
Functional Keywordscyanobacteria, circadium rhythms, nitrogen fixation, unknown function
Biological sourceCyanothece sp. ATCC 51142
Total number of polymer chains2
Total formula weight39459.21
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 citationBuchko, 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: 22289180
DOI: 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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