6iyt
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal Structure of the acyltransferase domain from second module 14 of salinomycin polyketide synthase== | |
+ | <StructureSection load='6iyt' size='340' side='right'caption='[[6iyt]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6iyt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IYT FirstGlance]. <br> | ||
+ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6iyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iyt OCA], [http://pdbe.org/6iyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iyt RCSB], [http://www.ebi.ac.uk/pdbsum/6iyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iyt ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6iyt" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Zhang, F]] | [[Category: Zhang, F]] | ||
[[Category: Zheng, J]] | [[Category: Zheng, J]] | ||
+ | [[Category: Acyltransferase]] | ||
+ | [[Category: Ethylhmalonyl-coenzyme some]] | ||
+ | [[Category: Polyketide]] | ||
+ | [[Category: Transferase]] |
Revision as of 05:50, 3 July 2019
Crystal Structure of the acyltransferase domain from second module 14 of salinomycin polyketide synthase
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