2qnz
From Proteopedia
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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== | ||
| - | <StructureSection load='2qnz' size='340' side='right' caption='[[2qnz]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2qnz' size='340' side='right'caption='[[2qnz]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2qnz]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2qnz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. 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> |
| - | </td></tr><tr id='ligand'><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></td></tr> | + | </td></tr><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> |
| - | <tr id='related'><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> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u6s|1u6s]], [[1hzp|1hzp]], [[1u6e|1u6e]], [[1hnj|1hnj]], [[1hnk|1hnk]], [[2qnx|2qnx]], [[2qny|2qny]], [[2qo0|2qo0]], [[2qo1|2qo1]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[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]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Acyl carrier protein synthase|Acyl carrier protein synthase]] | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Alhamadsheh, M]] | [[Category: Alhamadsheh, M]] | ||
[[Category: Musayev, F]] | [[Category: Musayev, F]] | ||
Revision as of 08:26, 25 June 2021
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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Categories: Large Structures | Alhamadsheh, M | Musayev, F | Reynolds, K A | Sachdeva, S | Scarsdale, J N | Wright, H T | Acyltransferase | Cytoplasm | Enzyme inhibitor complex | Fatty acid biosynthesis | Lipid synthesis | Mechanism based inhibitor | Multifunctional enzyme | Myobacterium tuberculosis | Structural basis for substrate specificity | Transferase
