4tkv: Difference between revisions

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==CO-bound Nitrogenase MoFe-protein from A. vinelandii==
==CO-bound Nitrogenase MoFe-protein from A. vinelandii==
<StructureSection load='4tkv' size='340' side='right' caption='[[4tkv]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='4tkv' size='340' side='right' caption='[[4tkv]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m1n|1m1n]], [[3u7q|3u7q]], [[4tku|4tku]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m1n|1m1n]], [[3u7q|3u7q]], [[4tku|4tku]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tkv RCSB], [http://www.ebi.ac.uk/pdbsum/4tkv PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkv OCA], [http://pdbe.org/4tkv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tkv RCSB], [http://www.ebi.ac.uk/pdbsum/4tkv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tkv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4tkv" style="background-color:#fffaf0;"></div>
==See Also==
*[[Nitrogenase|Nitrogenase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 19:58, 5 August 2016

CO-bound Nitrogenase MoFe-protein from A. vinelandiiCO-bound Nitrogenase MoFe-protein from A. vinelandii

Structural highlights

4tkv is a 4 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , ,
Activity:Nitrogenase, with EC number 1.18.6.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NIFD_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. [NIFK_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.

Publication Abstract from PubMed

The mechanism of nitrogenase remains enigmatic, with a major unresolved issue concerning how inhibitors and substrates bind to the active site. We report a crystal structure of carbon monoxide (CO)-inhibited nitrogenase molybdenum-iron (MoFe)-protein at 1.50 angstrom resolution, which reveals a CO molecule bridging Fe2 and Fe6 of the FeMo-cofactor. The mu2 binding geometry is achieved by replacing a belt-sulfur atom (S2B) and highlights the generation of a reactive iron species uncovered by the displacement of sulfur. The CO inhibition is fully reversible as established by regain of enzyme activity and reappearance of S2B in the 1.43 angstrom resolution structure of the reactivated enzyme. The substantial and reversible reorganization of the FeMo-cofactor accompanying CO binding was unanticipated and provides insights into a catalytically competent state of nitrogenase.

Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase.,Spatzal T, Perez KA, Einsle O, Howard JB, Rees DC Science. 2014 Sep 26;345(6204):1620-3. doi: 10.1126/science.1256679. PMID:25258081[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Spatzal T, Perez KA, Einsle O, Howard JB, Rees DC. Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase. Science. 2014 Sep 26;345(6204):1620-3. doi: 10.1126/science.1256679. PMID:25258081 doi:http://dx.doi.org/10.1126/science.1256679

4tkv, resolution 1.50Å

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