Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family
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.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE SC OFFICE OF BIOLOGICAL & ENVIRONMENTAL RESEARCH
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1049240
- Report Number(s):
- BNL-96930-2012-JA; FEBLAL; R&D Project: BO-070; KP1605010; TRN: US201217%%575
- Journal Information:
- FEBS Letters, Vol. 586, Issue 4; ISSN 0014-5793
- Country of Publication:
- United States
- Language:
- English
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Structural characterization of the protein cce_0567 from Cyanothece 51142, a metalloprotein associated with nitrogen fixation in the DUF683 family