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6k97
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==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]] | ||
Revision as of 06:47, 27 November 2019
Crystal structure of fusion DH domain
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