2qny: Difference between revisions
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[[Image: | ==Crystal structure of the complex between the A246F mutant of mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and SS-(2-hydroxyethyl) O-decyl ester carbono(dithioperoxoic) acid== | ||
<StructureSection load='2qny' size='340' side='right' caption='[[2qny]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2qny]] 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=2QNY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QNY FirstGlance]. <br> | |||
</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> | |||
<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]], [[2qnz|2qnz]], [[2qo0|2qo0]], [[2qo1|2qo1]]</td></tr> | |||
<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> | |||
<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> | |||
<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=2qny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qny OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qny RCSB], [http://www.ebi.ac.uk/pdbsum/2qny PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/2qny_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:18420147</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]] | *[[Acyl carrier protein synthase|Acyl carrier protein synthase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
Revision as of 07:10, 29 September 2014
Crystal structure of the complex between the A246F mutant of mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and SS-(2-hydroxyethyl) O-decyl ester carbono(dithioperoxoic) acid
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Beta-ketoacyl-acyl-carrier-protein synthase I
- Mycobacterium tuberculosis
- Alhamadsheh, M.
- Musayev, F.
- Reynolds, K A.
- Sachdeva, S.
- Scarsdale, J N.
- Wright, H T.
- Acyltransferase
- Enzyme inhibitor complex
- Fatty acid biosynthesis
- Lipid synthesis
- Mechanism based inhibitor
- Multifunctional enzyme
- Myobacterium tuberculosis
- Structural basis for substrate specificity
- Transferase
