1mio

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spinqualitylabelsall models 1mio, resolution 3.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION

Overview

The crystal structure of the nitrogenase molybdenum-iron (MoFe) protein, from Clostridium pasteurianum (Cp1) has been determined at 3.0-A, resolution by a combination of isomorphous replacement, molecular, replacement, and noncrystallographic symmetry averaging. The structure of, Cp1, including the two types of metal centers associated with the protein, (the FeMo-cofactor and the P-cluster pair), is similar to that previously, described for the MoFe-protein from Azotobacter vinelandii (Av1). Unique, features of the Cp1 structure arise from the presence of an approximately, 50-residue insertion in the alpha subunit and an approximately 50-residue, deletion in the beta subunit. As a consequence, the FeMo-cofactor is more, buried in Cp1 than in Av1, since the insertion is located on the surface, above the FeMo-cofactor. The location of this insertion near the putative, nitrogenase iron protein binding site provides a structural basis for the, observation that the nitrogenase proteins from C. pasteurianum have low, activity with complementary nitrogenase proteins isolated from other, organisms. Mechanistic implications of the Cp1 structure for substrate, entry/product release, substrate binding to the FeMo-cofactor, and, electron- and proton-transfer reactions of nitrogenase are discussed.

About this Structure

1MIO is a Protein complex structure of sequences from Clostridium pasteurianum with CA, HCA, CFM and CLP as ligands. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution., Kim J, Woo D, Rees DC, Biochemistry. 1993 Jul 20;32(28):7104-15. PMID:8393705

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