1M1N

Nitrogenase MoFe protein from Azotobacter vinelandii

Summary for 1M1N

• Entry DOI: 10.2210/pdb1m1n/pdb
• Related: 1n2c 2min 3min
• Descriptor: Nitrogenase molybdenum-iron protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, 3-HYDROXY-3-CARBOXY-ADIPIC ACID, ... (7 entities in total)
• Functional Keywords: atomic resolution, femo cofactor, nitrogen fixation, central nitrogen ligand, oxidoreductase
• Biological source: Azotobacter vinelandii; More
• Total number of polymer chains: 8
• Total formula weight: 465373.69

Authors

Einsle, O.,Tezcan, F.A.,Andrade, S.L.A.,Schmid, B.,Yoshida, M.,Howard, J.B.,Rees, D.C. (deposition date: 2002-06-19, release date: 2002-09-11, Last modification date: 2024-02-14)

Primary citation

Einsle, O.,Tezcan, F.A.,Andrade, S.L.,Schmid, B.,Yoshida, M.,Howard, J.B.,Rees, D.C.
Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.
Science, 297:1696-1700, 2002

PubMed Abstract: A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.

PubMed: 12215645
DOI: 10.1126/science.1073877

Experimental method

X-RAY DIFFRACTION (1.16 Å)