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1y7l

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(New page: 200px<br /><applet load="1y7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y7l, resolution 1.55&Aring;" /> '''O-Acetylserine Sulfh...)
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[[Image:1y7l.gif|left|200px]]<br /><applet load="1y7l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1y7l, resolution 1.55&Aring;" />
 
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'''O-Acetylserine Sulfhydrylase Complex'''<br />
 
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==Overview==
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==O-Acetylserine Sulfhydrylase Complex==
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The biosynthesis of cysteine in bacteria and plants is carried out by a, two-step pathway, catalyzed by serine acetyltransferase (SAT) and, O-acetylserine sulfhydrylase (OASS; O-acetylserine [thiol] lyase). The, aerobic form of OASS forms a tight bienzyme complex with SAT in vivo, termed cysteine synthase. We have determined the crystal structure of OASS, in complex with a C-terminal peptide of SAT required for bienzyme complex, formation. The binding site of the peptide is at the active site of OASS, and its C-terminal carboxyl group occupies the same anion binding pocket, as the alpha-carboxylate of the O-acetylserine substrate of OASS. These, results explain the partial inhibition of OASS by SAT on complex formation, as well as the competitive dissociation of the complex by O-acetylserine.
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<StructureSection load='1y7l' size='340' side='right'caption='[[1y7l]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1y7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] and [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y7L FirstGlance]. <br>
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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]] 1.55&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1y7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y7l OCA], [https://pdbe.org/1y7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y7l RCSB], [https://www.ebi.ac.uk/pdbsum/1y7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y7l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYSK_HAEIN CYSK_HAEIN]
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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/y7/1y7l_consurf.spt"</scriptWhenChecked>
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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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</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=1y7l 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 biosynthesis of cysteine in bacteria and plants is carried out by a two-step pathway, catalyzed by serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS; O-acetylserine [thiol] lyase). The aerobic form of OASS forms a tight bienzyme complex with SAT in vivo, termed cysteine synthase. We have determined the crystal structure of OASS in complex with a C-terminal peptide of SAT required for bienzyme complex formation. The binding site of the peptide is at the active site of OASS, and its C-terminal carboxyl group occupies the same anion binding pocket as the alpha-carboxylate of the O-acetylserine substrate of OASS. These results explain the partial inhibition of OASS by SAT on complex formation as well as the competitive dissociation of the complex by O-acetylserine.
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==About this Structure==
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The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase.,Huang B, Vetting MW, Roderick SL J Bacteriol. 2005 May;187(9):3201-5. PMID:15838047<ref>PMID:15838047</ref>
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1Y7L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y7L OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase., Huang B, Vetting MW, Roderick SL, J Bacteriol. 2005 May;187(9):3201-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15838047 15838047]
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</div>
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[[Category: Cysteine synthase]]
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<div class="pdbe-citations 1y7l" 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>
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
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[[Category: Protein complex]]
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[[Category: Haemophilus influenzae Rd KW20]]
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[[Category: Huang, B.]]
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[[Category: Large Structures]]
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[[Category: Roderick, S.L.]]
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[[Category: Huang B]]
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[[Category: Vetting, M.W.]]
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[[Category: Roderick SL]]
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[[Category: SO4]]
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[[Category: Vetting MW]]
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[[Category: x-ray crystallography; sulfhydrylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:37:13 2007''
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Current revision

O-Acetylserine Sulfhydrylase Complex

PDB ID 1y7l

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