2kv1

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{{STRUCTURE_2kv1| PDB=2kv1 | SCENE= }}
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==Insights into Function, Catalytic Mechanism and Fold Evolution of Mouse Selenoprotein Methionine Sulfoxide Reductase B1 through Structural Analysis==
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===Insights into Function, Catalytic Mechanism and Fold Evolution of Mouse Selenoprotein Methionine Sulfoxide Reductase B1 through Structural Analysis===
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<StructureSection load='2kv1' size='340' side='right' caption='[[2kv1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_20605785}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2kv1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2kao 2kao]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KV1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=2kv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kv1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kv1 RCSB], [http://www.ebi.ac.uk/pdbsum/2kv1 PDBsum]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kv/2kv1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Methionine sulfoxide reductases protect cells by repairing oxidatively damaged methionine residues in proteins. Here, we report the first three-dimensional structure of the mammalian selenoprotein methionine sulfoxide reductase B1 (MsrB1), determined by high resolution NMR spectroscopy. Heteronuclear multidimensional spectra yielded NMR spectral assignments for the reduced form of MsrB1 in which catalytic selenocysteine (Sec) was replaced with cysteine (Cys). MsrB1 consists of a central structured core of two beta-sheets and a highly flexible, disordered N-terminal region. Analysis of pH dependence of NMR signals of catalytically relevant residues, comparison with the data for bacterial MsrBs, and NMR-based structural analysis of methionine sulfoxide (substrate) and methionine sulfone (inhibitor) binding to MsrB1 at the atomic level reveal a mechanism involving catalytic Sec(95) and resolving Cys(4) residues in catalysis. The MsrB1 structure differs from the structures of Cys-containing MsrBs in the use of distal selenenylsulfide, residues needed for catalysis, and the mode in which the active form of the enzyme is regenerated. In addition, this is the first structure of a eukaryotic zinc-containing MsrB, which highlights the structural role of this metal ion bound to four conserved Cys. We integrated this information into a structural model of evolution of MsrB superfamily.
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==About this Structure==
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Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis.,Aachmann FL, Sal LS, Kim HY, Marino SM, Gladyshev VN, Dikiy A J Biol Chem. 2010 Oct 22;285(43):33315-23. Epub 2010 Jul 5. PMID:20605785<ref>PMID:20605785</ref>
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[[2kv1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2kao 2kao]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KV1 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:020605785</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Lk3 transgenic mice]]
[[Category: Lk3 transgenic mice]]
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[[Category: Aachmann, F L.]]
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[[Category: Aachmann, F L]]
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[[Category: Dikiy, A.]]
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[[Category: Dikiy, A]]
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[[Category: Gladyshev, V N.]]
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[[Category: Gladyshev, V N]]
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[[Category: Kim, H Y.]]
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[[Category: Kim, H Y]]
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[[Category: Sal, L S.]]
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[[Category: Sal, L S]]
[[Category: Metal-binding]]
[[Category: Metal-binding]]
[[Category: Msrb1]]
[[Category: Msrb1]]

Revision as of 06:47, 22 December 2014

Insights into Function, Catalytic Mechanism and Fold Evolution of Mouse Selenoprotein Methionine Sulfoxide Reductase B1 through Structural Analysis

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