9f48: Difference between revisions

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'''Unreleased structure'''


The entry 9f48 is ON HOLD  until sometime in the future
==KS + AT di-domain of polyketide synthase 13 in Mycobacterium tuberculosis==
 
<StructureSection load='9f48' size='340' side='right'caption='[[9f48]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
Authors: Johnston, H.E., Futterer, K.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9f48]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9F48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9F48 FirstGlance]. <br>
Description: KS + AT di-domain of polyketide synthase 13 in Mycobacterium tuberculosis
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9f48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9f48 OCA], [https://pdbe.org/9f48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9f48 RCSB], [https://www.ebi.ac.uk/pdbsum/9f48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9f48 ProSAT]</span></td></tr>
[[Category: Futterer, K]]
</table>
[[Category: Johnston, H.E]]
== Function ==
[https://www.uniprot.org/uniprot/PKS13_MYCTU PKS13_MYCTU] Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:23770708, PubMed:25467124). Forms, with FadD32, the initiation module of the mycolic condensation system (PubMed:19436070, PubMed:19477415, PubMed:25467124). Synthesizes, in coupled reaction with FadD32, the biosynthetic precursors of mycolic acids, alpha-alkyl beta-ketoacids, via the condensation of two long chain fatty acid derivatives, a very long meromycoloyl-AMP and a shorter 2-carboxyacyl-CoA (PubMed:19436070, PubMed:25467124). The acyl chain of the acyl-AMP produced by FadD32 is specifically transferred onto the N-terminal ACP domain of Pks13, and then transferred onto the KS domain. The extender unit carboxyacyl-CoA is specifically loaded onto the AT domain, which catalyzes the covalent attachment of the carboxyacyl chain to its active site, and its subsequent transfer onto the P-pant arm of the C-terminal ACP domain. The KS domain catalyzes the condensation between the two loaded fatty acyl chains to produce an alpha-alkyl beta-ketothioester linked to the C-ACP domain (PubMed:19436070). Then, the thioesterase-like domain acts as a transacylase and is responsible for both the release and the transfer of the alpha-alkyl beta-ketoacyl chain onto a polyol acceptor molecule, particularly trehalose, leading to the formation of the trehalose monomycolate precursor (PubMed:25467124).<ref>PMID:19436070</ref> <ref>PMID:19477415</ref> <ref>PMID:23770708</ref> <ref>PMID:25467124</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Futterer K]]
[[Category: Johnston HE]]
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