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| | <StructureSection load='6k97' size='340' side='right'caption='[[6k97]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6k97' size='340' side='right'caption='[[6k97]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k97]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K97 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cmiP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1321967 Streptomyces sp. MJ635-86F5])</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'>[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> | + | <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> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptomyces sp. mj635-86f5]] | + | [[Category: Streptomyces sp. MJ635-86F5]] |
| - | [[Category: Chisuga, T]] | + | [[Category: Chisuga T]] |
| - | [[Category: Eguchi, T]] | + | [[Category: Eguchi T]] |
| - | [[Category: Kawasaki, D]] | + | [[Category: Kawasaki D]] |
| - | [[Category: Kudo, F]] | + | [[Category: Kudo F]] |
| - | [[Category: Miyanaga, A]] | + | [[Category: Miyanaga A]] |
| - | [[Category: Cremimycin biosynthesis]]
| + | |
| - | [[Category: Dehydratase]]
| + | |
| - | [[Category: Double hot dog fold]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Polyketide synthase]]
| + | |
| Structural highlights
Function
X5IJ93_9ACTN X5IY86_9ACTN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kawasaki D, Miyanaga A, Chisuga T, Kudo F, Eguchi T. Functional and Structural Analyses of the Split-Dehydratase Domain in the Biosynthesis of Macrolactam Polyketide Cremimycin. Biochemistry. 2019 Nov 18. doi: 10.1021/acs.biochem.9b00897. PMID:31721563 doi:http://dx.doi.org/10.1021/acs.biochem.9b00897
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