4WZB

Crystal Structure of MgAMPPCP-bound Av2-Av1 complex

Replaces:  2AFK

Summary for 4WZB

• Entry DOI: 10.2210/pdb4wzb/pdb
• Related: 2AFK
• Descriptor: Nitrogenase molybdenum-iron protein alpha chain, IRON/SULFUR CLUSTER, Nitrogenase molybdenum-iron protein beta chain, ... (11 entities in total)
• Functional Keywords: nitrogen fixation, iron-sulfur, metal-binding, molybdenum, oxidoreductase
• Biological source: Azotobacter vinelandii; More
• Total number of polymer chains: 8
• Total formula weight: 351295.18

Authors

Tezcan, F.A.,Kaiser, J.T.,Mustafi, D.,Walton, M.Y.,Howard, J.B.,Rees, D.C. (deposition date: 2014-11-19, release date: 2015-02-25, Last modification date: 2024-02-28)

Primary citation

Tezcan, F.A.,Kaiser, J.T.,Mustafi, D.,Walton, M.Y.,Howard, J.B.,Rees, D.C.
Nitrogenase complexes: multiple docking sites for a nucleotide switch protein.
Science, 309:1377-1380, 2005

PubMed Abstract: 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.

PubMed: 16123301
DOI: 10.1126/science.1115653

Experimental method

X-RAY DIFFRACTION (2.3 Å)