6k97: Difference between revisions
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==Crystal structure of fusion DH domain== | |||
<StructureSection load='6k97' size='340' side='right'caption='[[6k97]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6k97]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K97 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6k97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k97 OCA], [http://pdbe.org/6k97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k97 RCSB], [http://www.ebi.ac.uk/pdbsum/6k97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k97 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In the biosynthesis of the macrolactam antibiotic cremimycin, the 3-aminononanoic acid starter unit is formed via a non-2-enoyl acyl carrier protein thioester intermediate, which is presumed to be constructed by cis-acyltransferase (AT) polyketide synthases (PKSs) CmiP2, CmiP3, and CmiP4. While canonical cis-AT PKS modules are comprised of a single polypeptide, the PKS module formed by CmiP2 and CmiP3 is split within the dehydratase (DH) domain. Here, we report the enzymatic function and the structural features of this split-DH domain. In vitro analysis showed that the split-DH domain catalyzes the dehydration reaction of (R)-3-hydroxynonanoyl N-acetylcysteamine thioester (SNAC) to form (E)-non-2-enoyl-SNAC, suggesting that the split-DH domain is catalytically active in cremimycin biosynthesis. In addition, structural analysis revealed that the CmiP2 and CmiP3 subunits of the split-DH domain form a tightly associated heterodimer through several hydrogen bonding and hydrophobic interactions, which are similar to those of canonical DH domains of other cis-AT PKSs. These results indicate that the split-DH domain has the same function and structure as common cis-AT PKS DH domains. | |||
Functional and Structural Analyses of the Split-Dehydratase Domain in the Biosynthesis of Macrolactam Polyketide Cremimycin.,Kawasaki D, Miyanaga A, Chisuga T, Kudo F, Eguchi T Biochemistry. 2019 Nov 18. doi: 10.1021/acs.biochem.9b00897. PMID:31721563<ref>PMID:31721563</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6k97" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chisuga, T]] | |||
[[Category: Eguchi, T]] | |||
[[Category: Kawasaki, D]] | |||
[[Category: Kudo, F]] | |||
[[Category: Miyanaga, A]] | |||
[[Category: Cremimycin biosynthesis]] | |||
[[Category: Dehydratase]] | |||
[[Category: Double hot dog fold]] | |||
[[Category: Lyase]] | |||
[[Category: Polyketide synthase]] | |||
