2j89: Difference between revisions
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==Functional and structural aspects of poplar cytosolic and plastidial type A methionine sulfoxide reductases== | |||
<StructureSection load='2j89' size='340' side='right'caption='[[2j89]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2j89]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Poptr Poptr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J89 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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=2j89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j89 OCA], [https://pdbe.org/2j89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j89 RCSB], [https://www.ebi.ac.uk/pdbsum/2j89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j89 ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j8/2j89_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2j89 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. In both enzymes, five cysteines, at positions 46, 81, 100, 196, and 202, are conserved. Biochemical and enzymatic analyses of the cysteine-mutated MsrAs support a catalytic mechanism involving three cysteines at positions 46, 196, and 202. Cys(46) is the catalytic cysteine, and the two C-terminal cysteines, Cys(196) and Cys(202), are implicated in the thioredoxin-dependent recycling mechanism. Inspection of the pMsrA x-ray three-dimensional structure, which has been determined in this study, strongly suggests that contrary to bacterial and Bos taurus MsrAs, which also contain three essential Cys, the last C-terminal Cys(202), but not Cys(196), is the first recycling cysteine that forms a disulfide bond with the catalytic Cys(46). Then Cys(202) forms a disulfide bond with the second recycling cysteine Cys(196) that is preferentially reduced by thioredoxin. In agreement with this assumption, Cys(202) is located closer to Cys(46) compared with Cys(196) and is included in a (202)CYG(204) signature specific for most plant MsrAs. The tyrosine residue corresponds to the one described to be involved in substrate binding in bacterial and B. taurus MsrAs. In these MsrAs, the tyrosine residue belongs to a similar signature as found in plant MsrAs but with the first C-terminal cysteine instead of the last C-terminal cysteine. | |||
Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases.,Rouhier N, Kauffmann B, Tete-Favier F, Palladino P, Gans P, Branlant G, Jacquot JP, Boschi-Muller S J Biol Chem. 2007 Feb 2;282(5):3367-78. Epub 2006 Nov 29. PMID:17135266<ref>PMID:17135266</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2j89" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Boschi-Muller, S | [[Category: Poptr]] | ||
[[Category: Branlant, G | [[Category: Boschi-Muller, S]] | ||
[[Category: Gans, P | [[Category: Branlant, G]] | ||
[[Category: Jacquot, J P | [[Category: Gans, P]] | ||
[[Category: Kauffmann, B | [[Category: Jacquot, J P]] | ||
[[Category: Palladino, P | [[Category: Kauffmann, B]] | ||
[[Category: Rouhier, N | [[Category: Palladino, P]] | ||
[[Category: Tete-Favier, F | [[Category: Rouhier, N]] | ||
[[Category: Tete-Favier, F]] | |||
[[Category: Msra]] | [[Category: Msra]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Poplar]] | [[Category: Poplar]] | ||
[[Category: Sulfoxide reductase]] | [[Category: Sulfoxide reductase]] | ||
Latest revision as of 11:04, 19 January 2022
Functional and structural aspects of poplar cytosolic and plastidial type A methionine sulfoxide reductasesFunctional and structural aspects of poplar cytosolic and plastidial type A methionine sulfoxide reductases
Structural highlights
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 PubMedThe genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. In both enzymes, five cysteines, at positions 46, 81, 100, 196, and 202, are conserved. Biochemical and enzymatic analyses of the cysteine-mutated MsrAs support a catalytic mechanism involving three cysteines at positions 46, 196, and 202. Cys(46) is the catalytic cysteine, and the two C-terminal cysteines, Cys(196) and Cys(202), are implicated in the thioredoxin-dependent recycling mechanism. Inspection of the pMsrA x-ray three-dimensional structure, which has been determined in this study, strongly suggests that contrary to bacterial and Bos taurus MsrAs, which also contain three essential Cys, the last C-terminal Cys(202), but not Cys(196), is the first recycling cysteine that forms a disulfide bond with the catalytic Cys(46). Then Cys(202) forms a disulfide bond with the second recycling cysteine Cys(196) that is preferentially reduced by thioredoxin. In agreement with this assumption, Cys(202) is located closer to Cys(46) compared with Cys(196) and is included in a (202)CYG(204) signature specific for most plant MsrAs. The tyrosine residue corresponds to the one described to be involved in substrate binding in bacterial and B. taurus MsrAs. In these MsrAs, the tyrosine residue belongs to a similar signature as found in plant MsrAs but with the first C-terminal cysteine instead of the last C-terminal cysteine. Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases.,Rouhier N, Kauffmann B, Tete-Favier F, Palladino P, Gans P, Branlant G, Jacquot JP, Boschi-Muller S J Biol Chem. 2007 Feb 2;282(5):3367-78. Epub 2006 Nov 29. PMID:17135266[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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