6q93

From Proteopedia

(Difference between revisions)

Current revision

MgADP-bound Fe protein of Vanadium nitrogenase from Azotobacter vinelandii

Structural highlights

6q93 is a 8 chain structure with sequence from Azotobacter vinelandii DJ. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C1DI30_AZOVD The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.[HAMAP-Rule:MF_00533]

Publication Abstract from PubMed

Nitrogenases catalyze the biological fixation of inert N2 into bioavailable ammonium. They are bipartite systems consisting of the catalytic dinitrogenase and a complementary reductase, the Fe protein that is also the site where ATP is hydrolyzed to drive the reaction forward. Three different subclasses of dinitrogenases are known, employing either molybdenum, vanadium or only iron at their active site cofactor. Although in all these classes the mode and mechanism of interaction with Fe protein is conserved, each one encodes its own orthologue of the reductase in the corresponding gene cluster. Here we present the 2.2 A resolution structure of VnfH from Azotobacter vinelandii, the Fe protein of the alternative, vanadium-dependent nitrogenase system, in its ADP-bound state. VnfH adopts the same conformation that was observed for NifH, the Fe protein of molybdenum nitrogenase, in complex with ADP, representing a state of the functional cycle that is ready for reduction and subsequent nucleotide exchange. The overall similarity of NifH and VnfH confirms the experimentally determined cross-reactivity of both ATP-hydrolyzing reductases.

Crystal structure of VnfH, the iron protein component of vanadium nitrogenase.,Rohde M, Trncik C, Sippel D, Gerhardt S, Einsle O J Biol Inorg Chem. 2018 Oct;23(7):1049-1056. doi: 10.1007/s00775-018-1602-4. Epub, 2018 Aug 23. PMID:30141094^[1]

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

References

↑ Rohde M, Trncik C, Sippel D, Gerhardt S, Einsle O. Crystal structure of VnfH, the iron protein component of vanadium nitrogenase. J Biol Inorg Chem. 2018 Oct;23(7):1049-1056. doi: 10.1007/s00775-018-1602-4. Epub, 2018 Aug 23. PMID:30141094 doi:http://dx.doi.org/10.1007/s00775-018-1602-4

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6q93"

Categories: Azotobacter vinelandii DJ | Large Structures | Einsle O | Gerhardt S | Rohde M

@@ Line 1: / Line 1: @@
 ==MgADP-bound Fe protein of Vanadium nitrogenase from Azotobacter vinelandii==
-<StructureSection load='6q93' size='340' side='right' caption='[[6q93]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='6q93' size='340' side='right'caption='[[6q93]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6q93]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii_(strain_dj_/_atcc_baa-1303) Azotobacter vinelandii (strain dj / atcc baa-1303)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q93 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6q93]] 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=6Q93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q93 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.2&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=6q93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q93 OCA], [http://pdbe.org/6q93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q93 RCSB], [http://www.ebi.ac.uk/pdbsum/6q93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q93 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=6q93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q93 OCA], [https://pdbe.org/6q93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q93 RCSB], [https://www.ebi.ac.uk/pdbsum/6q93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q93 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/C1DI30_AZOVD C1DI30_AZOVD]] The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.[HAMAP-Rule:MF_00533]
+[https://www.uniprot.org/uniprot/C1DI30_AZOVD C1DI30_AZOVD] The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.[HAMAP-Rule:MF_00533]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 6q93" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Nitrogenase]]
+[[Category: Azotobacter vinelandii DJ]]
-[[Category: Einsle, O]]
+[[Category: Large Structures]]
-[[Category: Gerhardt, S]]
+[[Category: Einsle O]]
-[[Category: Rohde, M]]
+[[Category: Gerhardt S]]
-[[Category: Biological nitrogen fixation]]
+[[Category: Rohde M]]
-[[Category: Dinitrogenase reductase]]
-[[Category: Electron transport]]
-[[Category: Fe protein]]
-[[Category: Vanadium nitrogenase]]
-[[Category: Vnfh]]

6q93

From Proteopedia

Current revision

MgADP-bound Fe protein of Vanadium nitrogenase from Azotobacter vinelandii

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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