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 A° 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. 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.
Revised: July 23, 2012 |
Published: February 17, 2012
Citation
Buchko G.W., and H. Robinson. 2012.Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family.FEBS Letters 586, no. 4:350-355.PNNL-SA-84898.doi:10.1016/j.febslet.2012.01.037