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1l1d

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[[Image:1l1d.gif|left|200px]]
 
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{{Structure
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==Crystal structure of the C-terminal methionine sulfoxide reductase domain (MsrB) of N. gonorrhoeae pilB==
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|PDB= 1l1d |SIZE=350|CAPTION= <scene name='initialview01'>1l1d</scene>, resolution 1.85&Aring;
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<StructureSection load='1l1d' size='340' side='right'caption='[[1l1d]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1l1d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L1D FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-methionine-(S)-S-oxide_reductase L-methionine-(S)-S-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.13 1.8.4.13] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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|GENE= pilB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 Neisseria gonorrhoeae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1d OCA], [https://pdbe.org/1l1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l1d RCSB], [https://www.ebi.ac.uk/pdbsum/1l1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1d ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1d OCA], [http://www.ebi.ac.uk/pdbsum/1l1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l1d RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/MSRAB_NEIGO MSRAB_NEIGO] 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.[HAMAP-Rule:MF_01400]
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== Evolutionary Conservation ==
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'''Crystal structure of the C-terminal methionine sulfoxide reductase domain (MsrB) of N. gonorrhoeae pilB'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l1d_consurf.spt"</scriptWhenChecked>
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Methionine sulfoxide reductases (Msr) protect against oxidative damage that can contribute to cell death. The tandem Msr domains (MsrA and MsrB) of the pilB protein from Neisseria gonorrhoeae each reduce different epimeric forms of methionine sulfoxide. The overall fold of the MsrB domain revealed by the 1.85 A crystal structure shows no resemblance to the previously determined MsrA structures from other organisms. Despite the lack of homology, the active sites show approximate mirror symmetry. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate. Unlike the MsrA domain, the MsrB domain activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. The collapse of the reaction intermediate most likely results in the formation of a sulfenic or selenenic acid moiety. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. These observations have broad implications for modular catalysis, antibiotic drug design and continuing longevity studies in mammals.
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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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==About this Structure==
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</jmolCheckbox>
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1L1D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1D OCA].
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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/main_output.php?pdb_ID=1l1d ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB., Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW, Nat Struct Biol. 2002 May;9(5):348-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11938352 11938352]
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</StructureSection>
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[[Category: L-methionine-(S)-S-oxide reductase]]
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[[Category: Large Structures]]
[[Category: Neisseria gonorrhoeae]]
[[Category: Neisseria gonorrhoeae]]
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[[Category: Single protein]]
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[[Category: Brot N]]
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[[Category: Brot, N.]]
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[[Category: Etienne F]]
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[[Category: Etienne, F.]]
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[[Category: Lowther WT]]
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[[Category: Lowther, W T.]]
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[[Category: Matthews BW]]
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[[Category: Matthews, B W.]]
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[[Category: Weissbach H]]
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[[Category: Weissbach, H.]]
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[[Category: cacodylate complex]]
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[[Category: cys-arg-asp catalytic triad]]
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[[Category: met-r(o) reductase]]
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[[Category: msrb]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:36 2008''
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Current revision

Crystal structure of the C-terminal methionine sulfoxide reductase domain (MsrB) of N. gonorrhoeae pilB

PDB ID 1l1d

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