6k97: Difference between revisions

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'''Unreleased structure'''


The entry 6k97 is ON HOLD  until Paper Publication
==Crystal structure of fusion DH domain==
<StructureSection load='6k97' size='340' side='right'caption='[[6k97]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6k97]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._MJ635-86F5 Streptomyces sp. MJ635-86F5]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6K97 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6k97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k97 OCA], [https://pdbe.org/6k97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k97 RCSB], [https://www.ebi.ac.uk/pdbsum/6k97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k97 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/X5IJ93_9ACTN X5IJ93_9ACTN] [https://www.uniprot.org/uniprot/X5IY86_9ACTN X5IY86_9ACTN]
<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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6k97" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. MJ635-86F5]]
[[Category: Chisuga T]]
[[Category: Eguchi T]]
[[Category: Kawasaki D]]
[[Category: Kudo F]]
[[Category: Miyanaga A]]
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