4ndp

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'''Unreleased structure'''
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==Crystal structure Molybdenum Storage Protein with fully Mo-loaded cavity==
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<StructureSection load='4ndp' size='340' side='right' caption='[[4ndp]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ndp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NDP FirstGlance]. <br>
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</td></tr><tr><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=M10:(MU3-OXO)-TRIS(MU2-OXO)-NONAKISOXO-TRIMOLYBDENUM+(VI)'>M10</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ogx|2ogx]], [[4f6t|4f6t]], [[4ndo|4ndo]], [[4ndq|4ndq]], [[4ndr|4ndr]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ndp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ndp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ndp RCSB], [http://www.ebi.ac.uk/pdbsum/4ndp PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The molybdenum storage protein (MoSto) can store more than 100 Mo or W atoms as discrete polyoxometalate (POM) clusters. Here, we describe the three POM cluster sites along the threefold axis of the protein complex based on four X-ray structures with slightly different polyoxomolybdate compositions between 1.35 and 2A resolution. In contrast to the Moalpha-out binding site occupied by an Mo3 cluster, the Moalpha-in and Mobeta binding sites contain rather weak and non-uniform electron density for the Mo atoms (but clearly identifiable by anomalous data), suggesting the presence of POM cluster ensembles and/or degradation products of larger aggregates. The "Moalpha-in cluster ensemble" was interpreted as an antiprism-like Mo6 species superimposed with an Mo7 pyramide and the "Mobeta cluster ensemble" as an Mo13 cluster (present mostly in a degraded form) composed of a pyramidal Mo7 and a Mo3 building block linked by three spatially separated MoOx units. Inside the ball-shaped Mo13 cluster sits an occluded central atom, perhaps a metal ion. POM cluster formation at the Moalpha-in and Mobeta sites appears to be driven by filtering out and binding/protecting self-assembled transient species complementary to the protein template.
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The entry 4ndp is ON HOLD
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Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein.,Poppe J, Warkentin E, Demmer U, Kowalewski B, Dierks T, Schneider K, Ermler U J Inorg Biochem. 2014 Sep;138:122-8. doi: 10.1016/j.jinorgbio.2014.05.009. Epub, 2014 May 28. PMID:24945101<ref>PMID:24945101</ref>
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Authors: Poppe, J., Warkentin, E., Demmer, U., Ermler, U.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure Molybdenum Storage Protein with fully Mo-loaded cavity
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Azotobacter vinelandii]]
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[[Category: Demmer, U.]]
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[[Category: Ermler, U.]]
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[[Category: Poppe, J.]]
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[[Category: Warkentin, E.]]
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[[Category: Atp binding]]
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[[Category: Metal binding protein]]
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[[Category: Molybdenum binding]]
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[[Category: Molybdenum storage]]
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[[Category: Rossman fold]]

Revision as of 08:57, 13 August 2014

Crystal structure Molybdenum Storage Protein with fully Mo-loaded cavity

4ndp, resolution 1.60Å

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