1d6s

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[[Image:1d6s.gif|left|200px]]<br /><applet load="1d6s" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d6s, resolution 2.30&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE K41A MUTANT OF O-ACETYLSERINE SULFHYDRYLASE COMPLEXED IN EXTERNAL ALDIMINE LINKAGE WITH METHIONINE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE K41A MUTANT OF O-ACETYLSERINE SULFHYDRYLASE COMPLEXED IN EXTERNAL ALDIMINE LINKAGE WITH METHIONINE==
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Covalent binding of L-methionine as an external aldimine to the pyridoxal 5'-phosphate-cofactor in the K41A mutant of O-acetylserine sulfhydrylase from Salmonella typhimurium induces a large conformational change in the protein. Methionine mimics the action of the substrate O-acetyl-L-serine during catalysis. The alpha-carboxylate moiety of L-methionine in external aldimine linkage with the active site pyridoxal 5'-phosphate forms a hydrogen bonding network to the "asparagine-loop" P67-T68-N69-G70 which adopts a different conformation than in the native protein. The side-chain nitrogen of Asn69 moves more than 7 A to make a hydrogen bond to the alpha-carboxylate group of the inhibitor. As the external aldimine is formed, the PLP tilts by 13 degrees along its longitudinal axis such that C4' moves toward the entrance to the active site and the side-chain of the methionine is directed toward the active site entrance. The local rearrangement acts as a trigger to induce a large global conformational change in the protein. A subdomain comprised of beta-strand 4, alpha-helix 3, beta-strand 5 and alpha-helix 4 moves towards the active site by a rotation of 7 degrees. This subdomain movement results in a reduction of the severe twist of its central beta-sheet and reduces the active site entrance to a small hole, giving access only to small molecules like sulfide, the second substrate, or acetate, the first product.
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<StructureSection load='1d6s' size='340' side='right'caption='[[1d6s]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1d6s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D6S FirstGlance]. <br>
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1D6S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=MET:'>MET</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1D6S OCA].
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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]] 2.3&#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=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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==Reference==
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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=1d6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6s OCA], [https://pdbe.org/1d6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d6s RCSB], [https://www.ebi.ac.uk/pdbsum/1d6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d6s ProSAT]</span></td></tr>
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Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium., Burkhard P, Tai CH, Ristroph CM, Cook PF, Jansonius JN, J Mol Biol. 1999 Aug 27;291(4):941-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10452898 10452898]
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</table>
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[[Category: Cysteine synthase]]
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== Function ==
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[[Category: Salmonella typhimurium]]
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[https://www.uniprot.org/uniprot/CYSK_SALTY CYSK_SALTY] 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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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Burkhard, P.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Cook, P F.]]
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Check<jmol>
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[[Category: Jansonius, J N.]]
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<jmolCheckbox>
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[[Category: Ristroph, C M.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d6/1d6s_consurf.spt"</scriptWhenChecked>
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[[Category: Tai, C H.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: MET]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: PLP]]
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</jmolCheckbox>
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[[Category: beta replacement enzyme]]
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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=1d6s ConSurf].
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[[Category: cysteine biosynthesis]]
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<div style="clear:both"></div>
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[[Category: k41a]]
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__TOC__
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[[Category: plp]]
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</StructureSection>
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[[Category: Large Structures]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:36 2008''
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Burkhard P]]
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[[Category: Cook PF]]
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[[Category: Jansonius JN]]
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[[Category: Ristroph CM]]
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[[Category: Tai CH]]

Current revision

CRYSTAL STRUCTURE OF THE K41A MUTANT OF O-ACETYLSERINE SULFHYDRYLASE COMPLEXED IN EXTERNAL ALDIMINE LINKAGE WITH METHIONINE

PDB ID 1d6s

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