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| | ==Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (reduced form)== | | ==Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (reduced form)== |
| - | <StructureSection load='3hcg' size='340' side='right' caption='[[3hcg]], [[Resolution|resolution]] 1.82Å' scene=''> | + | <StructureSection load='3hcg' size='340' side='right'caption='[[3hcg]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hcg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimd Neimd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HCG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hcg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_A Neisseria meningitidis serogroup A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HCG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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">[[3hch|3hch]], [[3hci|3hci]], [[3hcj|3hcj]]</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=3hcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hcg OCA], [https://pdbe.org/3hcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hcg RCSB], [https://www.ebi.ac.uk/pdbsum/3hcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hcg ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrAB, NMA0290, pilB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=65699 NEIMD])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-methionine_(R)-S-oxide_reductase Peptide-methionine (R)-S-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.12 1.8.4.12] </span></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=3hcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hcg OCA], [http://pdbe.org/3hcg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hcg RCSB], [http://www.ebi.ac.uk/pdbsum/3hcg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hcg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MSRAB_NEIMA MSRAB_NEIMA]] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | + | [https://www.uniprot.org/uniprot/MSRAB_NEIMA MSRAB_NEIMA] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/3hcg_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/3hcg_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Neimd]] | + | [[Category: Large Structures]] |
| - | [[Category: Favier, F]] | + | [[Category: Neisseria meningitidis serogroup A]] |
| - | [[Category: Kauffmann, B]] | + | [[Category: Favier F]] |
| - | [[Category: Ranaivoson, F M]]
| + | [[Category: Kauffmann B]] |
| - | [[Category: Disulfide bond]] | + | [[Category: Ranaivoson FM]] |
| - | [[Category: Electron transport]] | + | |
| - | [[Category: Methionine sulfoxide reductase b]]
| + | |
| - | [[Category: Multifunctional enzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Pilb]]
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| - | [[Category: Redox-active center]]
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| - | [[Category: Reduced form]]
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| - | [[Category: Transport]]
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| Structural highlights
Function
MSRAB_NEIMA Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Methionine sulfoxide reductases (Msrs) are enzymes that catalyze the reduction of methionine sulfoxide back to methionine. In vivo, Msrs are essential in the protection of cells against oxidative damage to proteins and in the virulence of some bacteria. Two structurally unrelated classes of Msrs, named MsrA and MsrB, exist. MsrB are stereospecific to R epimer on the sulfur of sulfoxide. All MsrB share a common reductase step with the formation of a sulfenic acid intermediate. For the subclass of MsrB whose recycling process passes through the formation of an intradisulfide bond, the recycling reducer is thioredoxin. In the present study, X-ray structures of Neisseria meningitidis MsrB have been determined. The structures have a fold based on two beta-sheets, similar to the fold already described for other MsrB, with the recycling Cys63 located in a position favorable for disulfide bond formation with the catalytic Cys117. X-ray structures of Xanthomonas campestris MsrB have also been determined. In the C117S MsrB structure with a bound substrate, the recycling Cys31 is far from Ser117, with Trp65 being essential in the reductase step located in between. This positioning prevents the formation of the Cys31-Cys117 disulfide bond. In the oxidized structure, a drastic conformational reorganization of the two beta-sheets due to withdrawal of the Trp65 region from the active site, which remains compatible with an efficient thioredoxin-recycling process, is observed. The results highlight the remarkable structural malleability of the MsrB fold.
Methionine sulfoxide reductase B displays a high level of flexibility.,Ranaivoson FM, Neiers F, Kauffmann B, Boschi-Muller S, Branlant G, Favier F J Mol Biol. 2009 Nov 20;394(1):83-93. Epub 2009 Sep 4. PMID:19733575[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ranaivoson FM, Neiers F, Kauffmann B, Boschi-Muller S, Branlant G, Favier F. Methionine sulfoxide reductase B displays a high level of flexibility. J Mol Biol. 2009 Nov 20;394(1):83-93. Epub 2009 Sep 4. PMID:19733575 doi:10.1016/j.jmb.2009.08.073
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