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4k5s

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==The crystal structure of premithramycin B in complex with MTMOIV, a baeyer-villiger monooxygenase from the mithramycin biosynthetic pathway in streptomyces argillaceus.==
==The crystal structure of premithramycin B in complex with MTMOIV, a baeyer-villiger monooxygenase from the mithramycin biosynthetic pathway in streptomyces argillaceus.==
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<StructureSection load='4k5s' size='340' side='right' caption='[[4k5s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='4k5s' size='340' side='right'caption='[[4k5s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4k5s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_argillaceus"_routien "streptomyces argillaceus" routien]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K5S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K5S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4k5s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_argillaceus Streptomyces argillaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K5S FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PM0:PREMITHRAMYCIN+B'>PM0</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k5r|4k5r]]</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PM0:PREMITHRAMYCIN+B'>PM0</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mtmOIV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=41951 "Streptomyces argillaceus" Routien])</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=4k5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k5s OCA], [https://pdbe.org/4k5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k5s RCSB], [https://www.ebi.ac.uk/pdbsum/4k5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k5s ProSAT]</span></td></tr>
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<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=4k5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k5s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k5s RCSB], [http://www.ebi.ac.uk/pdbsum/4k5s PDBsum]</span></td></tr>
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</table>
</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/Q194P4_STRAA Q194P4_STRAA]
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Baeyer-Villiger monooxygenases (BVMOs) have been shown to play key roles for the biosynthesis of important natural products. MtmOIV, a homodimeric FAD- and NADPH-dependent BVMO, catalyzes the key frame-modifying steps of the mithramycin biosynthetic pathway, including an oxidative C-C bond cleavage, by converting its natural substrate premithramycin B into mithramycin DK, the immediate precursor of mithramycin. The drastically improved protein structure of MtmOIV along with the high-resolution structure of MtmOIV in complex with its natural substrate premithramycin B are reported here, revealing previously undetected key residues that are important for substrate recognition and catalysis. Kinetic analyses of selected mutants allowed us to probe the substrate binding pocket of MtmOIV and also to discover the putative NADPH binding site. This is the first substrate-bound structure of MtmOIV providing new insights into substrate recognition and catalysis, which paves the way for the future design of a tailored enzyme for the chemo-enzymatic preparation of novel mithramycin analogues.
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Molecular Insight into Substrate Recognition and Catalysis of Baeyer-Villiger Monooxygenase MtmOIV, the Key Frame-Modifying Enzyme in the Biosynthesis of Anticancer Agent Mithramycin.,Bosserman MA, Downey T, Noinaj N, Buchanan SK, Rohr J ACS Chem Biol. 2013 Sep 13. PMID:23992662<ref>PMID:23992662</ref>
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From MEDLINE&reg;/PubMed&reg;, 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: Streptomyces argillaceus routien]]
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[[Category: Large Structures]]
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[[Category: Bosserman, M A.]]
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[[Category: Streptomyces argillaceus]]
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[[Category: Buchanan, S K.]]
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[[Category: Bosserman MA]]
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[[Category: Noinaj, N.]]
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[[Category: Buchanan SK]]
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[[Category: Rohr, J.]]
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[[Category: Noinaj N]]
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[[Category: Baeyer-villiger]]
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[[Category: Rohr J]]
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[[Category: Fad binding protein]]
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[[Category: Flavin binding protein]]
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[[Category: Mithramycin]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]
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[[Category: Rossmann fold]]
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Current revision

The crystal structure of premithramycin B in complex with MTMOIV, a baeyer-villiger monooxygenase from the mithramycin biosynthetic pathway in streptomyces argillaceus.

PDB ID 4k5s

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