1m1o

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(New page: 200px<br /><applet load="1m1o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m1o, resolution 1.95&Aring;" /> '''Crystal structure of...)
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[[Image:1m1o.jpg|left|200px]]<br /><applet load="1m1o" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m1o, resolution 1.95&Aring;" />
 
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'''Crystal structure of biosynthetic thiolase, C89A mutant, complexed with acetoacetyl-CoA'''<br />
 
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==Overview==
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==Crystal structure of biosynthetic thiolase, C89A mutant, complexed with acetoacetyl-CoA==
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Biosynthetic thiolase catalyzes the formation of acetoacetyl-CoA from two, molecules of acetyl-CoA. This is a key step in the synthesis of many, biological compounds, including steroid hormones and ketone bodies. The, thiolase reaction involves two chemically distinct steps; during acyl, transfer, an acetyl group is transferred from acetyl-CoA to Cys89, and in, the Claisen condensation step, this acetyl group is further transferred to, a second molecule of acetyl-CoA, generating acetoacetyl-CoA. Here, new, crystallographic data for Zoogloea ramigera biosynthetic thiolase are, presented, covering all intermediates of the thiolase catalytic cycle. The, high-resolution structures indicate that the acetyl group goes through, four conformations while being transferred from acetyl-CoA via the, acetylated enzyme to acetoacetyl-CoA. This transfer is catalyzed in a, rigid cavity lined by mostly hydrophobic side chains, in addition to the, catalytic residues Cys89, His348, and Cys378. The structures highlight the, importance of an oxyanion hole formed by a water molecule and His348 in, stabilizing the negative charge on the thioester oxygen atom of acetyl-CoA, at two different steps of the reaction cycle. Another oxyanion hole, composed of the main chain nitrogen atoms of Cys89 and Gly380, complements, a negative charge of the thioester oxygen anion of the acetylated, intermediate, stabilizing the tetrahedral transition state of the Claisen, condensation step. The reactivity of the active site may be modulated by, hydrogen bonding networks extending from the active site toward the back, of the molecule.
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<StructureSection load='1m1o' size='340' side='right'caption='[[1m1o]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m1o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Zoogloea_ramigera Zoogloea ramigera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1O 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]] 1.95&#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=CAA:ACETOACETYL-COENZYME+A'>CAA</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=1m1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1o OCA], [https://pdbe.org/1m1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1o RCSB], [https://www.ebi.ac.uk/pdbsum/1m1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THIL_SHIZO THIL_SHIZO]
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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/m1/1m1o_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=1m1o ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1M1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zoogloea_ramigera Zoogloea ramigera] with SO4 and CAA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M1O OCA].
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*[[Thiolase 3D structures|Thiolase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes., Kursula P, Ojala J, Lambeir AM, Wierenga RK, Biochemistry. 2002 Dec 31;41(52):15543-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12501183 12501183]
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[[Category: Large Structures]]
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[[Category: Acetyl-CoA C-acetyltransferase]]
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[[Category: Single protein]]
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[[Category: Zoogloea ramigera]]
[[Category: Zoogloea ramigera]]
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[[Category: Kursula, P.]]
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[[Category: Kursula P]]
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[[Category: Lambeir, A.M.]]
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[[Category: Lambeir A-M]]
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[[Category: Ojala, J.]]
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[[Category: Ojala J]]
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[[Category: Wierenga, R.K.]]
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[[Category: Wierenga RK]]
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[[Category: CAA]]
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[[Category: SO4]]
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[[Category: thiolase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:04:18 2007''
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Current revision

Crystal structure of biosynthetic thiolase, C89A mutant, complexed with acetoacetyl-CoA

PDB ID 1m1o

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