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 1.16&Aring;" /> '''Nitrogenase MoFe pro...)
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[[Image:1m1n.gif|left|200px]]<br /><applet load="1m1n" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m1n.gif|left|200px]]<br /><applet load="1m1n" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m1n, resolution 1.16&Aring;" />
caption="1m1n, resolution 1.16&Aring;" />
'''Nitrogenase MoFe protein from Azotobacter vinelandii'''<br />
'''Nitrogenase MoFe protein from Azotobacter vinelandii'''<br />
==Overview==
==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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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==
==About this Structure==
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1M1N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with CA, HCA, CLF and CFN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M1N OCA].
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1M1N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HCA:'>HCA</scene>, <scene name='pdbligand=CLF:'>CLF</scene> and <scene name='pdbligand=CFN:'>CFN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1N OCA].
==Reference==
==Reference==
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[[Category: Nitrogenase]]
[[Category: Nitrogenase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Andrade, S.L.A.]]
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[[Category: Andrade, S L.A.]]
[[Category: Einsle, O.]]
[[Category: Einsle, O.]]
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[[Category: Howard, J.B.]]
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[[Category: Howard, J B.]]
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[[Category: Rees, D.C.]]
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[[Category: Rees, D C.]]
[[Category: Schmid, B.]]
[[Category: Schmid, B.]]
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[[Category: Tezcan, F.A.]]
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[[Category: Tezcan, F A.]]
[[Category: Yoshida, M.]]
[[Category: Yoshida, M.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: nitrogen fixation]]
[[Category: nitrogen fixation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:04:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:33 2008''

Revision as of 11:50, 21 February 2008


1m1n, resolution 1.16Å

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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 , , and 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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