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5yk9

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m (Protected "5yk9" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5yk9 is ON HOLD until Oct 12 2019
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==Crystal structure of selenomethionine-labelled indole prenyltransferase AmbP1==
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<StructureSection load='5yk9' size='340' side='right' caption='[[5yk9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yk9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YK9 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5yk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yk9 OCA], [http://pdbe.org/5yk9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yk9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yk9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yk9 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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AmbP1 is a cyanobacterial aromatic prenyltransferase and a dedicated synthase for (R)-3-geranyl-3-isocyanovinyl indolenine (2), the biogenetic precursor for hapalindole-type alkaloids. The regioselective geranylation of cis-indolyl vinyl isonitrile (1) by the standalone AmbP1 to give 2 has been shown to require a magnesium ion (Mg(2+) ) to suppress the formation of cis-2-geranylindolyl vinyl isonitrile (3). Here, we report high-resolution crystal structures of AmbP1 in complex with 1 and geranyl S-thiodiphosphate (GSPP) in the presence and absence of a Mg(2+) effector. The comparative study of these structures revealed a unique allosteric binding site for Mg(2+) that modulates the conformation of 1 in the active site of AmbP1 for its selective geranylation. This work defines the structural basis for AmbP1 catalysis in the biogenesis of hapalindole-type alkaloids and provides the first atomic-level insight to the allosteric regulation of prenyltransferases.
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Authors:
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Molecular Insight into the Mg(2+) -Dependent Allosteric Control of Indole Prenylation by Aromatic Prenyltransferase AmbP1.,Awakawa T, Mori T, Nakashima Y, Zhai R, Wong CP, Hillwig ML, Liu X, Abe I Angew Chem Int Ed Engl. 2018 Jun 4;57(23):6810-6813. doi: 10.1002/anie.201800855., Epub 2018 May 7. PMID:29677386<ref>PMID:29677386</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5yk9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Abe, I]]
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[[Category: Awakawa, T]]
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[[Category: Liu, X]]
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[[Category: Nakashima, Y]]
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[[Category: Cyanobacteria]]
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[[Category: Transferase]]

Revision as of 05:53, 6 June 2018

Crystal structure of selenomethionine-labelled indole prenyltransferase AmbP1

5yk9, resolution 3.00Å

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