4f6t
From Proteopedia
(Difference between revisions)
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| - | + | ==The crystal structure of the molybdenum storage protein (MoSto) from Azotobacter vinelandii loaded with various polyoxometalates== | |
| - | + | <StructureSection load='4f6t' size='340' side='right' caption='[[4f6t]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4f6t]] 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=4F6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F6T FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6M0:MO(6)-O(26)+CLUSTER'>6M0</scene>, <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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ogx|2ogx]]</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=4f6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f6t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f6t RCSB], [http://www.ebi.ac.uk/pdbsum/4f6t PDBsum]</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. | [[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 == | ||
| + | Some N(2)-fixing bacteria prolong the functionality of nitrogenase in molybdenum starvation by a special Mo storage protein (MoSto) that can store more than 100 Mo atoms. The presented 1.6 A X-ray structure of MoSto from Azotobacter vinelandii reveals various discrete polyoxomolybdate clusters, three covalently and three noncovalently bound Mo(8), three Mo(5-7), and one Mo(3) clusters, and several low occupied, so far undefinable clusters, which are embedded in specific pockets inside a locked cage-shaped (alphabeta)(3) protein complex. The structurally identical Mo(8) clusters (three layers of two, four, and two MoO(n) octahedra) are distinguishable from the [Mo(8)O(26)](4-) cluster formed in acidic solutions by two displaced MoO(n) octahedra implicating three kinetically labile terminal ligands. Stabilization in the covalent Mo(8) cluster is achieved by Mo bonding to Hisalpha156-N(epsilon2) and Glualpha129-O(epsilon1). The absence of covalent protein interactions in the noncovalent Mo(8) cluster is compensated by a more extended hydrogen-bond network involving three pronounced histidines. One displaced MoO(n) octahedron might serve as nucleation site for an inhomogeneous Mo(5-7) cluster largely surrounded by bulk solvent. In the Mo(3) cluster located on the 3-fold axis, the three accurately positioned His140-N(epsilon2) atoms of the alpha subunits coordinate to the Mo atoms. The formed polyoxomolybdate clusters of MoSto, not detectable in bulk solvent, are the result of an interplay between self- and protein-driven assembly processes that unite inorganic supramolecular and protein chemistry in a host-guest system. Template, nucleation/protection, and catalyst functions of the polypeptide as well as perspectives for designing new clusters are discussed. | ||
| - | + | Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters.,Kowalewski B, Poppe J, Demmer U, Warkentin E, Dierks T, Ermler U, Schneider K J Am Chem Soc. 2012 Jun 13;134(23):9768-74. Epub 2012 May 31. PMID:22612644<ref>PMID:22612644</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
| - | [[Category: Demmer, U | + | [[Category: Demmer, U]] |
| - | [[Category: Ermler, U | + | [[Category: Ermler, U]] |
| - | [[Category: Kowalewski, B | + | [[Category: Kowalewski, B]] |
| - | [[Category: Poppe, J | + | [[Category: Poppe, J]] |
| - | [[Category: Schneider, K | + | [[Category: Schneider, K]] |
| - | [[Category: Warkentin, E | + | [[Category: Warkentin, E]] |
[[Category: Atp hydrolysis]] | [[Category: Atp hydrolysis]] | ||
[[Category: Atp hydrolyzation]] | [[Category: Atp hydrolyzation]] | ||
Revision as of 06:57, 25 December 2014
The crystal structure of the molybdenum storage protein (MoSto) from Azotobacter vinelandii loaded with various polyoxometalates
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