2afh

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spinqualitylabelsall models PDB ID 2afh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.10Å
Ligands:	, , , , , , , , , , and
Activity:	Nitrogenase, with EC number 1.18.6.1
Coordinates:	save as pdb, mmCIF, xml

Crystal Structure of Nucleotide-Free Av2-Av1 Complex

Overview

Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.

About this Structure

2AFH is a Protein complex structure of sequences from Azotobacter vinelandii. Full crystallographic information is available from OCA.

Reference

Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:16123301

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