View source for 5yk9


==Crystal structure of selenomethionine-labelled indole prenyltransferase AmbP1==
<StructureSection load='5yk9' size='340' side='right'caption='[[5yk9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yk9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fischerella_ambigua_UTEX_1903 Fischerella ambigua UTEX 1903]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5YK9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.001&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5yk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yk9 OCA], [https://pdbe.org/5yk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yk9 RCSB], [https://www.ebi.ac.uk/pdbsum/5yk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yk9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/V5TDZ4_FISAU V5TDZ4_FISAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yk9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fischerella ambigua UTEX 1903]]
[[Category: Large Structures]]
[[Category: Abe I]]
[[Category: Awakawa T]]
[[Category: Liu X]]
[[Category: Nakashima Y]]