4wza: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 4wza is ~~ON HOLD until Paper~~ Publication

==Asymmetric Nucleotide Binding in the Nitrogenase Complex==

== Structural highlights ==

<table><tr><td colspan='2'>[[4wza]] is a 8 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=4WZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZA FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8995Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4wza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wza OCA], [https://pdbe.org/4wza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wza RCSB], [https://www.ebi.ac.uk/pdbsum/4wza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wza ProSAT]</span></td></tr>

</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.

== Publication Abstract from PubMed ==

The roles of ATP hydrolysis in electron-transfer (ET) reactions of the nitrogenase catalytic cycle remain obscure. Here, we present a new structure of a nitrogenase complex crystallized with MgADP and MgAMPPCP, an ATP analogue. In this structure the two nucleotides are bound asymmetrically by the Fe-protein subunits connected to the two different MoFe-protein subunits. This binding mode suggests that ATP hydrolysis and phosphate release may proceed by a stepwise mechanism. Through the associated Fe-protein conformational changes, a stepwise mechanism is anticipated to prolong the lifetime of the Fe-protein-MoFe-protein complex and, in turn, could orchestrate the sequence of intracomplex ET required for substrate reduction.

~~Authors:~~ Tezcan~~, F.A.~~, Kaiser~~, J.T.~~, Howard, J.~~B., Rees, D.C~~.

Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase.,Tezcan FA, Kaiser JT, Howard JB, Rees DC J Am Chem Soc. 2014 Dec 23. PMID:25522159<ref>PMID:25522159</ref>

~~Description~~: ~~Asymmetric Nucleotide Binding in the~~ Nitrogenase ~~Complex~~

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

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Tezcan, F.A~~]]

[[Category: Kaiser~~, J.T~~]]

[[Category: ~~Howard, J.B~~]]

==See Also==

[[Category: ~~Rees, D.C~~]]

*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Azotobacter vinelandii]]

[[Category: Large Structures]]

[[Category: Howard JB]]

[[Category: Kaiser JT]]

[[Category: Rees DC]]

[[Category: Tezcan FA]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4wza is ON HOLD  until Paper Publication
+==Asymmetric Nucleotide Binding in the Nitrogenase Complex==
+<StructureSection load='4wza' size='340' side='right'caption='[[4wza]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4wza]] is a 8 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=4WZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZA FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8995&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4wza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wza OCA], [https://pdbe.org/4wza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wza RCSB], [https://www.ebi.ac.uk/pdbsum/4wza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wza ProSAT]</span></td></tr>
+</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 roles of ATP hydrolysis in electron-transfer (ET) reactions of the nitrogenase catalytic cycle remain obscure. Here, we present a new structure of a nitrogenase complex crystallized with MgADP and MgAMPPCP, an ATP analogue. In this structure the two nucleotides are bound asymmetrically by the Fe-protein subunits connected to the two different MoFe-protein subunits. This binding mode suggests that ATP hydrolysis and phosphate release may proceed by a stepwise mechanism. Through the associated Fe-protein conformational changes, a stepwise mechanism is anticipated to prolong the lifetime of the Fe-protein-MoFe-protein complex and, in turn, could orchestrate the sequence of intracomplex ET required for substrate reduction.
-Authors: Tezcan, F.A., Kaiser, J.T., Howard, J.B., Rees, D.C.
+Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase.,Tezcan FA, Kaiser JT, Howard JB, Rees DC J Am Chem Soc. 2014 Dec 23. PMID:25522159<ref>PMID:25522159</ref>
-Description: Asymmetric Nucleotide Binding in the Nitrogenase Complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Tezcan, F.A]]
+<div class="pdbe-citations 4wza" style="background-color:#fffaf0;"></div>
-[[Category: Kaiser, J.T]]
-[[Category: Howard, J.B]]
+==See Also==
-[[Category: Rees, D.C]]
+*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Azotobacter vinelandii]]
+[[Category: Large Structures]]
+[[Category: Howard JB]]
+[[Category: Kaiser JT]]
+[[Category: Rees DC]]
+[[Category: Tezcan FA]]