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 diazo- trophic cyanobacterium Cyanothece sp. ATCC 51142, was determined to 1.60 Å resolution. Cce_0566 is a homodimer with each molecule composed of eight a-helices folded on one side of a three strand anti-parallel b-sheet. Hydrophobic interactions between the side chains of largely conserved residues on the surface of each b-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. Finally, 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:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 1035403
- Report Number(s):
- PNNL-SA-84898; 14398; TRN: US201204%%574
- 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
Structural Characterization of the Protein cce_0567 from Cyanothece 51142, a Metalloprotein Associated with Nitrogen Fixation in the DUF683 Family