6guj
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6guj is ON HOLD Authors: Ermler, U., Poppe, J., Bruenle, S. Description: Molybdenum storage protein with two occupied ATP binding sites [[Category:...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Molybdenum storage protein with two occupied ATP binding sites== | |
| + | <StructureSection load='6guj' size='340' side='right' caption='[[6guj]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6guj]] is a 2 chain structure with sequence from [http://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=6GUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GUJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8M0:BIS(MU4-OXO)-TETRAKIS(MU3-OXO)-HEXAKIS(MU2-OXO)-HEXADECAOXO-OCTAMOLYBDENUM+(VI)'>8M0</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene>, <scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</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=6guj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6guj OCA], [http://pdbe.org/6guj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6guj RCSB], [http://www.ebi.ac.uk/pdbsum/6guj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6guj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MOSB_AZOVD MOSB_AZOVD]] Intracellular storage of molybdenum. Binds polyoxomolybdates. Can bind at least 90 molybdenum atoms per protein molecule. [[http://www.uniprot.org/uniprot/MOSA_AZOVD MOSA_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 == | ||
| + | A continuous FeMo-cofactor supply for nitrogenase maturation is ensured in Azotobacter vinelandii by developing a cage-like molybdenum storage protein (MoSto) capable to store ca. 120 molybdate molecules (MoO4 (2-) ) as discrete polyoxometalate (POM) clusters. To gain mechanistic insight into this process MoSto was characterized by Mo and ATP/ADP content, structural and kinetic analysis. We defined three functionally relevant states specified by the presence of both ATP/ADP and POM clusters (MoStofunct ), of only ATP/ADP (MoStobasal ) and of neither ATP/ADP nor POM clusters (MoStozero ), respectively. POM clusters are only produced when ATP is hydrolyzed to ADP and phosphate. Vmax was ca. 13 mumolphosphate min(-1) mg(-1) and Km for molybdate and ATP/Mg(2+) in the low micromolar range. ATP hydrolysis presumably proceeds at subunit alpha, which is compatible with a highly occupied alpha-ATP/Mg(2+) and a weaker occupied beta-ATP/no Mg(2+) binding site found in the MoStofunct structure. Several findings indicate that POM cluster storage is separated into a rapid ATP-hydrolysis dependent molybdate transport across the protein cage wall and a slow molybdate assembly induced by combined auto-catalytic and protein-driven processes. The cage interior, the location of the POM cluster depot, is locked in all three states and thus not rapidly accessible for molybdate from the outside. Based on Vmax the entire Mo storage process should be completed in less than 10 s but requires, according to the molybdate content analysis, ca. 15 min. Long-time incubation of MoStobasal with non-physiological high molybdate amounts implicates an equilibrium in and outside the cage and POM cluster self-formation without ATP hydrolysis. This article is protected by copyright. All rights reserved. | ||
| - | + | The Molybdenum Storage Protein: A soluble ATP hydrolysis dependent molybdate pump.,Poppe J, Brunle S, Hail R, Wiesemann K, Schneider K, Ermler U FEBS J. 2018 Oct 27. doi: 10.1111/febs.14684. PMID:30367742<ref>PMID:30367742</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6guj" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii dj]] | ||
[[Category: Bruenle, S]] | [[Category: Bruenle, S]] | ||
| + | [[Category: Ermler, U]] | ||
[[Category: Poppe, J]] | [[Category: Poppe, J]] | ||
| + | [[Category: Atp]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Molybdenum storage]] | ||
| + | [[Category: Polyoxomolybdate cluster]] | ||
Current revision
Molybdenum storage protein with two occupied ATP binding sites
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