6vxt: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Activated Nitrogenase MoFe-protein from Azotobacter vinelandii== | ==Activated Nitrogenase MoFe-protein from Azotobacter vinelandii== | ||
<StructureSection load='6vxt' size='340' side='right'caption='[[6vxt]]' scene=''> | <StructureSection load='6vxt' size='340' side='right'caption='[[6vxt]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VXT OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6vxt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VXT FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vxt OCA], [https://pdbe.org/6vxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vxt RCSB], [https://www.ebi.ac.uk/pdbsum/6vxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vxt ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/NIFD_AZOVI NIFD_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The enzyme nitrogenase uses a suite of complex metallocofactors to reduce dinitrogen (N2) to ammonia. Mechanistic details of this reaction remain sparse. We report a 1.83-angstrom crystal structure of the nitrogenase molybdenum-iron (MoFe) protein captured under physiological N2 turnover conditions. This structure reveals asymmetric displacements of the cofactor belt sulfurs (S2B or S3A and S5A) with distinct dinitrogen species in the two alphabeta dimers of the protein. The sulfur-displaced sites are distinct in the ability of protein ligands to donate protons to the bound dinitrogen species, as well as the elongation of either the Mo-O5 (carboxyl) or Mo-O7 (hydroxyl) distance that switches the Mo-homocitrate ligation from bidentate to monodentate. These results highlight the dynamic nature of the cofactor during catalysis and provide evidence for participation of all belt-sulfur sites in this process. | |||
Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase.,Kang W, Lee CC, Jasniewski AJ, Ribbe MW, Hu Y Science. 2020 Jun 19;368(6497):1381-1385. doi: 10.1126/science.aaz6748. PMID:32554596<ref>PMID:32554596</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6vxt" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Azotobacter vinelandii]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hu Y]] | [[Category: Hu Y]] | ||
[[Category: Kang W]] | [[Category: Kang W]] | ||
[[Category: Ribbe MW]] | [[Category: Ribbe MW]] | ||
Latest revision as of 11:22, 11 October 2023
Activated Nitrogenase MoFe-protein from Azotobacter vinelandiiActivated Nitrogenase MoFe-protein from Azotobacter vinelandii
Structural highlights
FunctionNIFD_AZOVI This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Publication Abstract from PubMedThe enzyme nitrogenase uses a suite of complex metallocofactors to reduce dinitrogen (N2) to ammonia. Mechanistic details of this reaction remain sparse. We report a 1.83-angstrom crystal structure of the nitrogenase molybdenum-iron (MoFe) protein captured under physiological N2 turnover conditions. This structure reveals asymmetric displacements of the cofactor belt sulfurs (S2B or S3A and S5A) with distinct dinitrogen species in the two alphabeta dimers of the protein. The sulfur-displaced sites are distinct in the ability of protein ligands to donate protons to the bound dinitrogen species, as well as the elongation of either the Mo-O5 (carboxyl) or Mo-O7 (hydroxyl) distance that switches the Mo-homocitrate ligation from bidentate to monodentate. These results highlight the dynamic nature of the cofactor during catalysis and provide evidence for participation of all belt-sulfur sites in this process. Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase.,Kang W, Lee CC, Jasniewski AJ, Ribbe MW, Hu Y Science. 2020 Jun 19;368(6497):1381-1385. doi: 10.1126/science.aaz6748. PMID:32554596[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||