2qny: Difference between revisions

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[[Image:2qny.png|left|200px]]


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==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==
The line below this paragraph, containing "STRUCTURE_2qny", creates the "Structure Box" on the page.
<StructureSection load='2qny' size='340' side='right'caption='[[2qny]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2qny]] 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=2QNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QNY FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</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>
{{STRUCTURE_2qny|  PDB=2qny  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qny OCA], [https://pdbe.org/2qny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qny RCSB], [https://www.ebi.ac.uk/pdbsum/2qny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qny ProSAT]</span></td></tr>
</table>
== 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 ==
[[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/main_output.php?pdb_ID=2qny 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.


===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===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2qny" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18420147}}, adds the Publication Abstract to the page
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18420147 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_18420147}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[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].
 
==Reference==
<ref group="xtra">PMID:18420147</ref><ref group="xtra">PMID:11278743</ref><ref group="xtra">PMID:15713483</ref><references group="xtra"/>
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Alhamadsheh, M.]]
[[Category: Alhamadsheh M]]
[[Category: Musayev, F.]]
[[Category: Musayev F]]
[[Category: Reynolds, K A.]]
[[Category: Reynolds KA]]
[[Category: Sachdeva, S.]]
[[Category: Sachdeva S]]
[[Category: Scarsdale, J N.]]
[[Category: Scarsdale JN]]
[[Category: Wright, H T.]]
[[Category: Wright HT]]
[[Category: Acyltransferase]]
[[Category: Cytoplasm]]
[[Category: Enzyme inhibitor complex]]
[[Category: Fatty acid biosynthesis]]
[[Category: Lipid synthesis]]
[[Category: Mechanism based inhibitor]]
[[Category: Multifunctional enzyme]]
[[Category: Myobacterium tuberculosis]]
[[Category: Structural basis for substrate specificity]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/2qny"