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1m1t

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[[Image:1m1t.jpg|left|200px]]
 
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{{Structure
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==Biosynthetic thiolase, Q64A mutant==
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|PDB= 1m1t |SIZE=350|CAPTION= <scene name='initialview01'>1m1t</scene>, resolution 1.94&Aring;
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<StructureSection load='1m1t' size='340' side='right'caption='[[1m1t]], [[Resolution|resolution]] 1.94&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=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1m1t]] 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=1M1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1T FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </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]] 1.94&#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=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=1m1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1t OCA], [https://pdbe.org/1m1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1t RCSB], [https://www.ebi.ac.uk/pdbsum/1m1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1t ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1dlu|1DLU]], [[1dlv|1DLV]], [[1qfl|1QFL]], [[1dm3|1DM3]], [[1m1o|1M1O]], [[1m3k|1M3K]], [[1m3z|1M3Z]], [[1m4s|1M4S]], [[1m4t|1M4T]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1t OCA], [http://www.ebi.ac.uk/pdbsum/1m1t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m1t RCSB]</span>
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== Function ==
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}}
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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/m1/1m1t_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=1m1t ConSurf].
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<div style="clear:both"></div>
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'''Biosynthetic thiolase, Q64A mutant'''
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==See Also==
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*[[Thiolase 3D structures|Thiolase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Large Structures]]
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==About this Structure==
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1M1T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zoogloea_ramigera Zoogloea ramigera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1T OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/12501183 12501183]
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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: thiolase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:10:14 2008''
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Current revision

Biosynthetic thiolase, Q64A mutant

PDB ID 1m1t

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