View source for 5xww


==Substrate-bound Structure of G355T/Q364H mutant of a Ketoreductase from amphotericin Polyketide Synthases==
<StructureSection load='5xww' size='340' side='right'caption='[[5xww]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xww]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_nodosus Streptomyces nodosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XWW 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]] 1.96&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8H6:~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2,4-bis(oxidanyl)butanoyl]amino]propanoylamino]ethyl]+(2~{R})-2-methyl-3-oxidanylidene-pentanethioate'>8H6</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5xww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xww OCA], [https://pdbe.org/5xww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xww RCSB], [https://www.ebi.ac.uk/pdbsum/5xww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xww ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93NW7_9ACTN Q93NW7_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ketoreductase (KR) domains of modular polyketide synthases (PKSs) control the stereochemistry of C2 methyl and C3 hydroxyl substituents of polyketide intermediates. To understand the molecular basis of stereocontrol exerted by KRs, the crystal structure of a KR from the second module of the amphotericin PKS (AmpKR2) complexed with NADP(+) and 2-methyl-3-oxopentanoyl-pantetheine was solved. This first ternary structure provides direct evidence to the hypothesis that a substrate enters into the active site of an A-type KR from the side opposite the coenzyme to generate an L-hydroxyl substituent. A comparison with the ternary complex of a G355T/Q364H mutant sheds light on the structural basis for stereospecificity toward the substrate C2 methyl substituent. Functional assays suggest the pantetheine handle shows obvious influence on the catalytic efficiency and the stereochemical outcome. Together, these findings extend our current understanding of the stereochemical control of PKS KR domains.

Substrate-bound structures of a ketoreductase from amphotericin modular polyketide synthase.,Liu C, Yuan M, Xu X, Wang L, Keatinge-Clay AT, Deng Z, Lin S, Zheng J J Struct Biol. 2018 Apr 4. pii: S1047-8477(18)30091-1. doi:, 10.1016/j.jsb.2018.04.001. PMID:29626512<ref>PMID:29626512</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xww" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces nodosus]]
[[Category: Liu C]]
[[Category: Zheng J]]