Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 A resolution: comparison with the Azotobacter vinelandii MoFe protein.

ABSTRACT: The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08 Å resolution by multiwavelength anomalous diffraction phasing. Cp1 and the ortholog from Azotobacter vinelandii (Av1) represent two distinct families of nitrogenases, differing primarily by a long insertion in the α-subunit and a deletion in the β-subunit of Cp1 relative to Av1. Comparison of these two MoFe protein structures at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase. The FeMo cofactors defining the active sites of the MoFe protein are essentially identical between the two proteins. The surrounding environment is also highly conserved, suggesting that this structural arrangement is crucial for ni

SUBMITTER: Zhang LM 

PROVIDER: S-EPMC4321486 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature