View source for 4rl1


==Structural and functional analysis of a loading acyltransferase from the avermectin modular polyketide synthase==
<StructureSection load='4rl1' size='340' side='right'caption='[[4rl1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rl1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avermitilis_MA-4680_=_NBRC_14893 Streptomyces avermitilis MA-4680 = NBRC 14893]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RL1 FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rl1 OCA], [https://pdbe.org/4rl1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rl1 RCSB], [https://www.ebi.ac.uk/pdbsum/4rl1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rl1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q79ZN1_STRAW Q79ZN1_STRAW] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The loading acyltransferase (AT) domains of modular polyketide synthases (PKSs) control the choice of starter units incorporated into polyketides and are therefore attractive targets for the engineering of modular PKSs. Here, we report the structural and biochemical characterizations of the loading AT from avermectin modular PKS, which accepts more than 40 carboxylic acids as alternative starter units for the biosynthesis of a series of congeners. This first structural analysis of loading ATs from modular PKSs revealed the molecular basis for the relaxed substrate specificity. Residues important for substrate binding and discrimination were predicted by modeling a substrate into the active site. A mutant with altered specificity toward a panel of synthetic substrate mimics was generated by site-directed mutagenesis of the active site residues. The hydrolysis of the N-acetylcysteamine thioesters of racemic 2-methylbutyric acid confirmed the stereospecificity of the avermectin loading AT for an S configuration at the C-2 position of the substrate. Together, these results set the stage for region-specific modification of polyketides through active site engineering of loading AT domains of modular PKSs.

Structural and Functional Analysis of the Loading Acyltransferase from Avermectin Modular Polyketide Synthase.,Wang F, Wang Y, Ji J, Zhou Z, Yu J, Zhu H, Su Z, Zhang L, Zheng J ACS Chem Biol. 2015 Jan 22. PMID:25581064<ref>PMID:25581064</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rl1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces avermitilis MA-4680 = NBRC 14893]]
[[Category: Wang F]]
[[Category: Wang Y]]
[[Category: Zheng J]]