2v03

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[[Image:2v03.jpg|left|200px]]
 
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{{Structure
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==High resolution structure and catalysis of an O-acetylserine sulfhydrylase==
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|PDB= 2v03 |SIZE=350|CAPTION= <scene name='initialview01'>2v03</scene>, resolution 1.33&Aring;
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<StructureSection load='2v03' size='340' side='right'caption='[[2v03]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Gol+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Cit+Binding+Site+For+Chain+A'>AC3</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[2v03]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V03 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47]
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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]] 1.33&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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}}
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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=2v03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v03 OCA], [https://pdbe.org/2v03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v03 RCSB], [https://www.ebi.ac.uk/pdbsum/2v03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v03 ProSAT]</span></td></tr>
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</table>
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'''HIGH RESOLUTION STRUCTURE AND CATALYSIS OF AN O-ACETYLSERINE SULFHYDRYLASE'''
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== Function ==
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[https://www.uniprot.org/uniprot/CYSM_ECOLI CYSM_ECOLI] Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.
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== Evolutionary Conservation ==
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==Overview==
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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/v0/2v03_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=2v03 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 ==
The crystal structure of the dimeric O-acetylserine sulfhydrylase isozyme B from Escherichia coli (CysM), complexed with the substrate analog citrate, has been determined at 1.33 A resolution by X-ray diffraction analysis. The C1-carboxylate of citrate was bound at the carboxylate position of O-acetylserine, whereas the C6-carboxylate adopted two conformations. The activity of the enzyme and of several active center mutants was determined using an assay based on O-acetylserine and thio-nitrobenzoate (TNB). The unnatural substrate TNB was modeled into the reported structure. The substrate model and the observed mutant activities may facilitate future protein engineering attempts designed to broaden the substrate spectrum of the enzyme. A comparison of the reported structure with previously published CysM structures revealed large conformational changes. One of the crystal forms contained two dimers, each of which comprised one subunit in a closed and one in an open conformation. Although the homodimer asymmetry was most probably caused by crystal packing, it indicates that the enzyme can adopt such a state in solution, which may be relevant for the catalytic reaction.
The crystal structure of the dimeric O-acetylserine sulfhydrylase isozyme B from Escherichia coli (CysM), complexed with the substrate analog citrate, has been determined at 1.33 A resolution by X-ray diffraction analysis. The C1-carboxylate of citrate was bound at the carboxylate position of O-acetylserine, whereas the C6-carboxylate adopted two conformations. The activity of the enzyme and of several active center mutants was determined using an assay based on O-acetylserine and thio-nitrobenzoate (TNB). The unnatural substrate TNB was modeled into the reported structure. The substrate model and the observed mutant activities may facilitate future protein engineering attempts designed to broaden the substrate spectrum of the enzyme. A comparison of the reported structure with previously published CysM structures revealed large conformational changes. One of the crystal forms contained two dimers, each of which comprised one subunit in a closed and one in an open conformation. Although the homodimer asymmetry was most probably caused by crystal packing, it indicates that the enzyme can adopt such a state in solution, which may be relevant for the catalytic reaction.
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==About this Structure==
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High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli.,Zocher G, Wiesand U, Schulz GE FEBS J. 2007 Oct;274(20):5382-9. Epub 2007 Sep 26. PMID:17894825<ref>PMID:17894825</ref>
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2V03 is a [[Single protein]] structure of sequence 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=2V03 OCA].
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==Reference==
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High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli., Zocher G, Wiesand U, Schulz GE, FEBS J. 2007 Oct;274(20):5382-9. Epub 2007 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17894825 17894825]
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[[Category: Cysteine synthase]]
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Schulz, G E.]]
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[[Category: Wiesand, U.]]
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[[Category: Zocher, G.]]
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[[Category: CIT]]
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[[Category: GOL]]
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[[Category: amino-acid biosynthesis]]
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[[Category: cysteine biosynthesis]]
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[[Category: enzymatic sythesis of novel compound]]
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[[Category: enzyme kinetic]]
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[[Category: pyridoxal phosphate]]
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[[Category: transferase]]
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[[Category: x-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:41:49 2008''
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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 2v03" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Schulz GE]]
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[[Category: Wiesand U]]
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[[Category: Zocher G]]

Current revision

High resolution structure and catalysis of an O-acetylserine sulfhydrylase

PDB ID 2v03

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