Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Buchko GW,Robinson H

doi

10.1016/j.febslet.2012.01.037

subject

Has Abstract

pub_date

2012-02-17 00:00:00

pages

350-5

issue

4

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00070-1

journal_volume

586

pub_type

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