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1m1n

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{{STRUCTURE_1m1n| PDB=1m1n | SCENE= }}
{{STRUCTURE_1m1n| PDB=1m1n | SCENE= }}
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'''Nitrogenase MoFe protein from Azotobacter vinelandii'''
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===Nitrogenase MoFe protein from Azotobacter vinelandii===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12215645 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12215645}}
==About this Structure==
==About this Structure==
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[[Category: Femo cofactor]]
[[Category: Femo cofactor]]
[[Category: Nitrogen fixation]]
[[Category: Nitrogen fixation]]
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Revision as of 20:01, 2 July 2008

Image:1m1n.png

Template:STRUCTURE 1m1n

Nitrogenase MoFe protein from Azotobacter vinelandii

Template:ABSTRACT PUBMED 12215645

About this Structure

1M1N is a Protein complex structure of sequences from Azotobacter vinelandii. 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

Page seeded by OCA on Wed Jul 2 23:01:24 2008

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