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3s3l

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==Crystal Structure of CerJ from Streptomyces tendae==
==Crystal Structure of CerJ from Streptomyces tendae==
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<StructureSection load='3s3l' size='340' side='right' caption='[[3s3l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3s3l' size='340' side='right'caption='[[3s3l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s3l]] 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=3S3L OCA]. <br>
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<table><tr><td colspan='2'>[[3s3l]] 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=3S3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S3L FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
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</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&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<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=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s3l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s3l RCSB], [http://www.ebi.ac.uk/pdbsum/3s3l PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3s3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s3l OCA], [https://pdbe.org/3s3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s3l RCSB], [https://www.ebi.ac.uk/pdbsum/3s3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s3l ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/H2L2M1_STRTE H2L2M1_STRTE]
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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.
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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<ref>PMID:22179067</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: As 4 1460]]
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[[Category: Large Structures]]
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[[Category: Bretschneider, T.]]
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[[Category: Streptomyces tendae]]
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[[Category: Hertweck, C.]]
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[[Category: Bretschneider T]]
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[[Category: Stehle, T.]]
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[[Category: Hertweck C]]
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[[Category: Zocher, G.]]
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[[Category: Stehle T]]
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[[Category: Acyltransferase]]
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[[Category: Zocher G]]
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[[Category: Dimethyl malonyl transfer]]
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[[Category: Fabh homologue]]
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[[Category: Ks iii homologue]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of CerJ from Streptomyces tendae

PDB ID 3s3l

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