View source for 6rke


==Molybdenum storage protein - P212121, ADP, molybdate==
<StructureSection load='6rke' size='340' side='right'caption='[[6rke]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rke]] is a 12 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=6RKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RKE 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8M0:BIS(MU4-OXO)-TETRAKIS(MU3-OXO)-HEXAKIS(MU2-OXO)-HEXADECAOXO-OCTAMOLYBDENUM+(VI)'>8M0</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=LHW:MO(10)-O(35)+Cluster'>LHW</scene>, <scene name='pdbligand=LJB:MO(8)-O(26)+Cluster'>LJB</scene>, <scene name='pdbligand=M10:(MU3-OXO)-TRIS(MU2-OXO)-NONAKISOXO-TRIMOLYBDENUM+(VI)'>M10</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6rke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rke OCA], [https://pdbe.org/6rke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rke RCSB], [https://www.ebi.ac.uk/pdbsum/6rke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rke ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MOSB_AZOVD MOSB_AZOVD] Intracellular storage of molybdenum. Binds polyoxomolybdates. Can bind at least 90 molybdenum atoms per protein molecule.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The molybdenum storage protein (MoSto) deposits large amounts of molybdenum as polyoxomolybdate clusters in a heterohexameric (alphabeta)3 cage-like protein complex under ATP consumption. Here, we suggest a unique mechanism for the ATP-powered molybdate pumping process based on X-ray crystallography, cryoelectron microscopy, hydrogen-deuterium exchange mass spectrometry, and mutational studies of MoSto from Azotobacter vinelandii First, we show that molybdate, ATP, and Mg(2+) consecutively bind into the open ATP-binding groove of the beta-subunit, which thereafter becomes tightly locked by fixing the previously disordered N-terminal arm of the alpha-subunit over the beta-ATP. Next, we propose a nucleophilic attack of molybdate onto the gamma-phosphate of beta-ATP, analogous to the similar reaction of the structurally related UMP kinase. The formed instable phosphoric-molybdic anhydride becomes immediately hydrolyzed and, according to the current data, the released and accelerated molybdate is pressed through the cage wall, presumably by turning aside the Metbeta149 side chain. A structural comparison between MoSto and UMP kinase provides valuable insight into how an enzyme is converted into a molecular machine during evolution. The postulated direct conversion of chemical energy into kinetic energy via an activating molybdate kinase and an exothermic pyrophosphatase reaction to overcome a proteinous barrier represents a novelty in ATP-fueled biochemistry, because normally, ATP hydrolysis initiates large-scale conformational changes to drive a distant process.

Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism.,Brunle S, Eisinger ML, Poppe J, Mills DJ, Langer JD, Vonck J, Ermler U Proc Natl Acad Sci U S A. 2019 Dec 6. pii: 1913031116. doi:, 10.1073/pnas.1913031116. PMID:31811022<ref>PMID:31811022</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rke" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Azotobacter vinelandii DJ]]
[[Category: Large Structures]]
[[Category: Bruenle S]]
[[Category: Ermler U]]