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| | <StructureSection load='3t8e' size='340' side='right'caption='[[3t8e]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3t8e' size='340' side='right'caption='[[3t8e]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1460 As 4.1460]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T8E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t8e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T8E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s3l|3s3l]], [[3t5y|3t5y]], [[3t6s|3t6s]]</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=3t8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t8e OCA], [https://pdbe.org/3t8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t8e RCSB], [https://www.ebi.ac.uk/pdbsum/3t8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t8e ProSAT]</span></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=3t8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t8e OCA], [http://pdbe.org/3t8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t8e RCSB], [http://www.ebi.ac.uk/pdbsum/3t8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t8e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/H2L2M1_STRTE H2L2M1_STRTE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 4 1460]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bretschneider, T]] | + | [[Category: Streptomyces tendae]] |
| - | [[Category: Hertweck, C]] | + | [[Category: Bretschneider T]] |
| - | [[Category: Stehle, T]] | + | [[Category: Hertweck C]] |
| - | [[Category: Zocher, G]] | + | [[Category: Stehle T]] |
| - | [[Category: Fabh-like fold]]
| + | [[Category: Zocher G]] |
| - | [[Category: O-malonyl transferase]]
| + | |
| - | [[Category: Thiloase superfamily]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
H2L2M1_STRTE
Publication Abstract from PubMed
Ketosynthases produce the carbon backbones of a vast number of biologically active polyketides by catalyzing Claisen condensations of activated acyl and malonyl building blocks. Here we report that a ketosynthase homolog from Streptomyces tendae, CerJ, unexpectedly forms malonyl esters during the biosynthesis of cervimycin, a glycoside antibiotic against methicillin-resistant Staphylococcus aureus (MRSA). Deletion of cerJ yielded a substantially more active cervimycin variant lacking the malonyl side chain, and in vitro biotransformations revealed that CerJ is capable of transferring malonyl, methylmalonyl and dimethylmalonyl units onto the glycoside. According to phylogenetic analyses and elucidation of the crystal structure, CerJ is functionally and structurally positioned between the ketosynthase catalyzing Claisen condensations and acyl-ACP shuttles, and it features a noncanonical catalytic triad. Site-directed mutagenesis and structures of CerJ in complex with substrates not only allowed us to establish a model for the reaction mechanism but also provided insights into the evolution of this important subclass of the thiolase superfamily.
A ketosynthase homolog uses malonyl units to form esters in cervimycin biosynthesis.,Bretschneider T, Zocher G, Unger M, Scherlach K, Stehle T, Hertweck C Nat Chem Biol. 2011 Dec 18. doi: 10.1038/nchembio.746. PMID:22179067[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bretschneider T, Zocher G, Unger M, Scherlach K, Stehle T, Hertweck C. A ketosynthase homolog uses malonyl units to form esters in cervimycin biosynthesis. Nat Chem Biol. 2011 Dec 18. doi: 10.1038/nchembio.746. PMID:22179067 doi:10.1038/nchembio.746
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