1m1n
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(New page: 200px<br /><applet load="1m1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m1n, resolution 1.16Å" /> '''Nitrogenase MoFe pro...)
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Revision as of 18:57, 20 November 2007
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Nitrogenase MoFe protein from Azotobacter vinelandii
Overview
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.
About this Structure
1M1N is a Protein complex structure of sequences from Azotobacter vinelandii with CA, HCA, CLF and CFN as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.
Reference
Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor., Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC, Science. 2002 Sep 6;297(5587):1696-700. PMID:12215645
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