2o8v

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[[Image:2o8v.gif|left|200px]]
 
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{{Structure
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==PAPS reductase in a covalent complex with thioredoxin C35A==
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|PDB= 2o8v |SIZE=350|CAPTION= <scene name='initialview01'>2o8v</scene>, resolution 3.000&Aring;
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<StructureSection load='2o8v' size='340' side='right'caption='[[2o8v]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2o8v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O8V FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] </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]] 3&#8491;</td></tr>
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|GENE= cysH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), trxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=2o8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8v OCA], [https://pdbe.org/2o8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o8v RCSB], [https://www.ebi.ac.uk/pdbsum/2o8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o8v ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1sur|1SUR]], [[2trx|2TRX]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8v OCA], [http://www.ebi.ac.uk/pdbsum/2o8v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o8v RCSB]</span>
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[https://www.uniprot.org/uniprot/CYSH_ECOLI CYSH_ECOLI] Reduction of activated sulfate into sulfite.[HAMAP-Rule:MF_00063]
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}}
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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/o8/2o8v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2o8v 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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The crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase in complex with E. coli thioredoxin 1 (Trx1) has been determined to 3.0 A resolution. The two proteins are covalently linked via a mixed disulfide that forms during nucleophilic attack of Trx's N-terminal cysteine on the Sgamma atom of the PAPS reductase S-sulfocysteine (E-Cys-Sgamma-SO3-), a central intermediate in the catalytic cycle. For the first time in a crystal structure, residues 235-244 in the PAPS reductase C-terminus are observed, depicting an array of interprotein salt bridges between Trx and the strictly conserved glutathione-like sequence, Glu238Cys239Gly240Leu241His242. The structure also reveals a Trx-binding surface adjacent to the active site cleft and regions of PAPS reductase associated with conformational change. Interaction at this site strategically positions Trx to bind the S-sulfated C-terminus and addresses the mechanism for requisite structural rearrangement of this domain. An apparent sulfite-binding pocket at the protein-protein interface explicitly orients the S-sulfocysteine Sgamma atom for nucleophilic attack in a subsequent step. Taken together, the structure of PAPS reductase in complex with Trx highlights the large structural rearrangement required to accomplish sulfonucleotide reduction and suggests a role for Trx in catalysis beyond the paradigm of disulfide reduction.
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'''PAPS reductase in a covalent complex with thioredoxin C35A'''
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3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle.,Chartron J, Shiau C, Stout CD, Carroll KS Biochemistry. 2007 Apr 3;46(13):3942-51. Epub 2007 Mar 13. PMID:17352498<ref>PMID:17352498</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2o8v" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase in complex with E. coli thioredoxin 1 (Trx1) has been determined to 3.0 A resolution. The two proteins are covalently linked via a mixed disulfide that forms during nucleophilic attack of Trx's N-terminal cysteine on the Sgamma atom of the PAPS reductase S-sulfocysteine (E-Cys-Sgamma-SO3-), a central intermediate in the catalytic cycle. For the first time in a crystal structure, residues 235-244 in the PAPS reductase C-terminus are observed, depicting an array of interprotein salt bridges between Trx and the strictly conserved glutathione-like sequence, Glu238Cys239Gly240Leu241His242. The structure also reveals a Trx-binding surface adjacent to the active site cleft and regions of PAPS reductase associated with conformational change. Interaction at this site strategically positions Trx to bind the S-sulfated C-terminus and addresses the mechanism for requisite structural rearrangement of this domain. An apparent sulfite-binding pocket at the protein-protein interface explicitly orients the S-sulfocysteine Sgamma atom for nucleophilic attack in a subsequent step. Taken together, the structure of PAPS reductase in complex with Trx highlights the large structural rearrangement required to accomplish sulfonucleotide reduction and suggests a role for Trx in catalysis beyond the paradigm of disulfide reduction.
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2O8V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8V OCA].
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__TOC__
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</StructureSection>
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==Reference==
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3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle., Chartron J, Shiau C, Stout CD, Carroll KS, Biochemistry. 2007 Apr 3;46(13):3942-51. Epub 2007 Mar 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17352498 17352498]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphoadenylyl-sulfate reductase (thioredoxin)]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Carroll KS]]
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[[Category: Carroll, K S.]]
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[[Category: Chartron J]]
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[[Category: Chartron, J.]]
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[[Category: Shiau C]]
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[[Category: Shiau, C.]]
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[[Category: Stout CD]]
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[[Category: Stout, C D.]]
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[[Category: disulfide crosslinked complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:14:21 2008''
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Current revision

PAPS reductase in a covalent complex with thioredoxin C35A

PDB ID 2o8v

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