View source for 6iyr


==Crystal Structure of the acyltransferase domain from module 8 of the salinomycin polyketide synthase==
<StructureSection load='6iyr' size='340' side='right'caption='[[6iyr]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iyr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albus_subsp._albus Streptomyces albus subsp. albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IYR 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=6iyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iyr OCA], [https://pdbe.org/6iyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iyr RCSB], [https://www.ebi.ac.uk/pdbsum/6iyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iyr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H1ZZT7_9ACTN H1ZZT7_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Salinomycin with antibacterial and anticoccidial activities is a commercial polyether polyketide widely used in animal husbandry as a food additive. Malonyl-CoA (MCoA), methylmalonyl-CoA (MMCoA), and ethylmalonyl-CoA (EMCoA) are used as extension units in its biosynthesis. To understand how the salinomycin modular polyketide synthase (PKS) strictly discriminates among these extension units, the acyltransferase (AT) domains selecting MCoA, MMCoA, and EMCoA were structurally characterized. Molecular dynamics simulations of the AT structures helped to reveal the key interactions involved in enzyme-substrate recognitions, which enabled the engineering of AT mutants with switched specificity. The catalytic efficiencies ( kcat/ Km) of these AT mutants are comparable with those of the wild-type AT domains. These results set the stage for engineering the AT substrate specificity of modular PKSs.

Structural Insights into the Substrate Specificity of Acyltransferases from Salinomycin Polyketide Synthase.,Zhang F, Shi T, Ji H, Ali I, Huang S, Deng Z, Min Q, Bai L, Zhao Y, Zheng J Biochemistry. 2019 Jun 19. doi: 10.1021/acs.biochem.9b00305. PMID:31199122<ref>PMID:31199122</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iyr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces albus subsp. albus]]
[[Category: Zhang F]]
[[Category: Zheng J]]