8bts

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:27, 19 June 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8bts]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii_DJ Azotobacter vinelandii DJ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BTS FirstGlance]. <br>
<table><tr><td colspan='2'>[[8bts]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii_DJ Azotobacter vinelandii DJ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BTS FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1CL:FE(8)-S(7)+CLUSTER,+OXIDIZED'>1CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.03&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1CL:FE(8)-S(7)+CLUSTER,+OXIDIZED'>1CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=SO4:SULFATE+ION'>SO4</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=8bts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bts OCA], [https://pdbe.org/8bts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bts RCSB], [https://www.ebi.ac.uk/pdbsum/8bts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bts ProSAT]</span></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=8bts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bts OCA], [https://pdbe.org/8bts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bts RCSB], [https://www.ebi.ac.uk/pdbsum/8bts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bts ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[https://www.uniprot.org/uniprot/C1DGZ7_AZOVD C1DGZ7_AZOVD] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.[ARBA:ARBA00002621]
+
[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 substrate-reducing proteins of all nitrogenases (MoFe, VFe, and FeFe) are organized as alpha(2)ss(2)(gamma(2)) multimers with two functional halves. While their dimeric organization could afford improved structural stability of nitrogenases in vivo, previous research has proposed both negative and positive cooperativity contributions with respect to enzymatic activity. Here, a 1.4 kDa peptide was covalently introduced in the proximity of the P cluster, corresponding to the Fe protein docking position. The Strep-tag carried by the added peptide simultaneously sterically inhibits electron delivery to the MoFe protein and allows the isolation of partially inhibited MoFe proteins (where the half-inhibited MoFe protein was targeted). We confirm that the partially functional MoFe protein retains its ability to reduce N(2) to NH(3), with no significant difference in selectivity over obligatory/parasitic H(2) formation. Our experiment concludes that wild-type nitrogenase exhibits negative cooperativity during the steady state regarding H(2) and NH(3) formation (under Ar or N(2)), with one-half of the MoFe protein inhibiting turnover in the second half. This emphasizes the presence and importance of long-range (&gt;95 A) protein-protein communication in biological N(2) fixation in Azotobacter vinelandii.
+
-
Nitrogen Fixation and Hydrogen Evolution by Sterically Encumbered Mo-Nitrogenase.,Cadoux C, Ratcliff D, Maslac N, Gu W, Tsakoumagkos I, Hoogendoorn S, Wagner T, Milton RD JACS Au. 2023 May 9;3(5):1521-1533. doi: 10.1021/jacsau.3c00165. eCollection 2023 , May 22. PMID:37234119<ref>PMID:37234119</ref>
+
==See Also==
-
 
+
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 8bts" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Nitrogenase MoFe protein from A. vinelandii alpha double mutant C45A/L158C

PDB ID 8bts

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8bts"
Personal tools