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2qo0

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Revision as of 07:30, 25 October 2017

Crystal structure of the complex between the A246F mutant of mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and 11-(decyldithiocarbonyloxy)-undecanoic acid

Structural highlights

2qo0 is a 2 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1hzp, 1u6e, 1u6s, 1hnj, 1hnk, 2qnx, 2qny, 2qnz, 2qo1
Gene:	fabH ("Bacillus tuberculosis" (Zopf 1883) Klein 1884)
Activity:	[acyl-carrier-protein_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number 2.3.1.41
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Mycobacterium tuberculosis FabH initiates type II fatty acid synthase-catalyzed formation of the long chain (C(16)-C(22)) acyl-coenzyme A (CoA) precursors of mycolic acids, which are major constituents of the bacterial cell envelope. Crystal structures of M. tuberculosis FabH (mtFabH) show the substrate binding site to be a buried, extended L-shaped channel with only a single solvent access portal. Entrance of an acyl-CoA substrate through the solvent portal would require energetically unfavorable reptational threading of the substrate to its reactive position. Using a class of FabH inhibitors, we have tested an alternative hypothesis that FabH exists in an "open" form during substrate binding and product release, and a "closed" form in which catalysis and intermediate steps occur. This hypothesis is supported by mass spectrometric analysis of the product profile and crystal structures of complexes of mtFabH with these inhibitors.

Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH.,Sachdeva S, Musayev FN, Alhamadsheh MM, Scarsdale JN, Wright HT, Reynolds KA Chem Biol. 2008 Apr;15(4):402-12. PMID:18420147^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Choi KH, Kremer L, Besra GS, Rock CO. Identification and substrate specificity of beta -ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis. J Biol Chem. 2000 Sep 8;275(36):28201-7. PMID:10840036 doi:http://dx.doi.org/10.1074/jbc.M003241200
↑ Sachdeva S, Musayev FN, Alhamadsheh MM, Scarsdale JN, Wright HT, Reynolds KA. Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH. Chem Biol. 2008 Apr;15(4):402-12. PMID:18420147 doi:10.1016/j.chembiol.2008.03.007

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qo0"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex between the A246F mutant of mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and 11-(decyldithiocarbonyloxy)-undecanoic acid==
 <StructureSection load='2qo0' size='340' side='right' caption='[[2qo0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><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 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
 <tr id='activity'><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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qo0 OCA], [http://pdbe.org/2qo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qo0 RCSB], [http://www.ebi.ac.uk/pdbsum/2qo0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qo0 OCA], [http://pdbe.org/2qo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qo0 RCSB], [http://www.ebi.ac.uk/pdbsum/2qo0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qo0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 2qo0" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
 == References ==
 <references/>
@@ Line 44: / Line 42: @@
 [[Category: Wright, H T]]
 [[Category: Acyltransferase]]
+[[Category: Cytoplasm]]
 [[Category: Enzyme inhibitor complex]]
 [[Category: Fatty acid biosynthesis]]

2qo0

From Proteopedia

Revision as of 07:30, 25 October 2017

Crystal structure of the complex between the A246F mutant of mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and 11-(decyldithiocarbonyloxy)-undecanoic acid

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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