2q0q

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[[Image:2q0q.jpg|left|200px]]
 
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{{Structure
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==Structure of the Native M. Smegmatis Aryl Esterase==
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|PDB= 2q0q |SIZE=350|CAPTION= <scene name='initialview01'>2q0q</scene>, resolution 1.50&Aring;
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<StructureSection load='2q0q' size='340' side='right'caption='[[2q0q]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[2q0q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q0Q FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arylesterase Arylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.2 3.1.1.2] </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]] 1.5&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=2q0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q0q OCA], [https://pdbe.org/2q0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q0q RCSB], [https://www.ebi.ac.uk/pdbsum/2q0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q0q ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2q0s|2q0s]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q0q OCA], [http://www.ebi.ac.uk/pdbsum/2q0q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q0q RCSB]</span>
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== Evolutionary Conservation ==
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}}
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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'''Structure of the Native M. Smegmatis Aryl Esterase'''
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q0/2q0q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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==Overview==
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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=2q0q 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 unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium smegmatis forms the mechanistic basis for favoring alcoholysis over hydrolysis in water. Unlike hydrolases that perform alcoholysis only under anhydrous conditions, MsAcT demonstrates alcoholysis in substantially aqueous media and, in the presence of hydrogen peroxide, has a perhydrolysis:hydrolysis ratio 50-fold greater than that of the best lipase tested. The crystal structures of the apoenzyme and an inhibitor-bound form have been determined to 1.5 A resolution. MsAcT is an octamer in the asymmetric unit and forms a tightly associated aggregate in solution. Relative to other structurally similar monomers, MsAcT contains several insertions that contribute to the oligomerization and greatly restrict the shape of the active site, thereby limiting its accessibility. These properties create an environment by which MsAcT can catalyze transesterification reactions in an aqueous medium and suggests how a serine hydrolase can be engineered to be an efficient acyltransferase.
The unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium smegmatis forms the mechanistic basis for favoring alcoholysis over hydrolysis in water. Unlike hydrolases that perform alcoholysis only under anhydrous conditions, MsAcT demonstrates alcoholysis in substantially aqueous media and, in the presence of hydrogen peroxide, has a perhydrolysis:hydrolysis ratio 50-fold greater than that of the best lipase tested. The crystal structures of the apoenzyme and an inhibitor-bound form have been determined to 1.5 A resolution. MsAcT is an octamer in the asymmetric unit and forms a tightly associated aggregate in solution. Relative to other structurally similar monomers, MsAcT contains several insertions that contribute to the oligomerization and greatly restrict the shape of the active site, thereby limiting its accessibility. These properties create an environment by which MsAcT can catalyze transesterification reactions in an aqueous medium and suggests how a serine hydrolase can be engineered to be an efficient acyltransferase.
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==About this Structure==
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Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions.,Mathews I, Soltis M, Saldajeno M, Ganshaw G, Sala R, Weyler W, Cervin MA, Whited G, Bott R Biochemistry. 2007 Aug 7;46(31):8969-79. Epub 2007 Jul 18. PMID:17636869<ref>PMID:17636869</ref>
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2Q0Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q0Q OCA].
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==Reference==
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Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions., Mathews I, Soltis M, Saldajeno M, Ganshaw G, Sala R, Weyler W, Cervin MA, Whited G, Bott R, Biochemistry. 2007 Aug 7;46(31):8969-79. Epub 2007 Jul 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17636869 17636869]
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[[Category: Arylesterase]]
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[[Category: Mycobacterium smegmatis]]
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[[Category: Single protein]]
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[[Category: Bott, R.]]
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[[Category: Cervin, M A.]]
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[[Category: Ganshaw, G.]]
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[[Category: Mathews, I I.]]
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[[Category: Sala, R.]]
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[[Category: Saldajeno, M.]]
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[[Category: Soltis, M.]]
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[[Category: Weyler, W.]]
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[[Category: Whited, G.]]
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[[Category: acyl transfer]]
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[[Category: aryl esterase]]
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[[Category: oligomeric enzyme]]
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[[Category: sgnh hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:43:13 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 2q0q" 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: Large Structures]]
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[[Category: Mycolicibacterium smegmatis]]
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[[Category: Bott R]]
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[[Category: Cervin MA]]
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[[Category: Ganshaw G]]
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[[Category: Mathews II]]
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[[Category: Sala R]]
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[[Category: Saldajeno M]]
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[[Category: Soltis M]]
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[[Category: Weyler W]]
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[[Category: Whited G]]

Current revision

Structure of the Native M. Smegmatis Aryl Esterase

PDB ID 2q0q

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