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2qnz

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==Crystal structure of the complex between the mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and SS-(2-hydroxyethyl)-O-decyl ester carbono(dithioperoxoic) acid==
==Crystal structure of the complex between the mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and SS-(2-hydroxyethyl)-O-decyl ester carbono(dithioperoxoic) acid==
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<StructureSection load='2qnz' size='340' side='right' caption='[[2qnz]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='2qnz' size='340' side='right'caption='[[2qnz]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2qnz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QNZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QNZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2qnz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QNZ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=DFD:DECYL+FORMATE'>DFD</scene><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]] 2.3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u6s|1u6s]], [[1hzp|1hzp]], [[1u6e|1u6e]], [[1hnj|1hnj]], [[1hnk|1hnk]], [[2qnx|2qnx]], [[2qny|2qny]], [[2qo0|2qo0]], [[2qo1|2qo1]]</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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=DFD:DECYL+FORMATE'>DFD</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</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=2qnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qnz OCA], [https://pdbe.org/2qnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qnz RCSB], [https://www.ebi.ac.uk/pdbsum/2qnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qnz ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qnz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qnz RCSB], [http://www.ebi.ac.uk/pdbsum/2qnz PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/FABH_MYCTU FABH_MYCTU] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall.<ref>PMID:10840036</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/2qnz_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/2qnz_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2qnz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2qnz" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
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[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Alhamadsheh, M.]]
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[[Category: Alhamadsheh M]]
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[[Category: Musayev, F.]]
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[[Category: Musayev F]]
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[[Category: Reynolds, K A.]]
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[[Category: Reynolds KA]]
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[[Category: Sachdeva, S.]]
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[[Category: Sachdeva S]]
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[[Category: Scarsdale, J N.]]
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[[Category: Scarsdale JN]]
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[[Category: Wright, H T.]]
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[[Category: Wright HT]]
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[[Category: Acyltransferase]]
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[[Category: Enzyme inhibitor complex]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Lipid synthesis]]
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[[Category: Mechanism based inhibitor]]
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[[Category: Multifunctional enzyme]]
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[[Category: Myobacterium tuberculosis]]
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[[Category: Structural basis for substrate specificity]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the complex between the mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and SS-(2-hydroxyethyl)-O-decyl ester carbono(dithioperoxoic) acid

PDB ID 2qnz

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