View source for 5y72


==DMSPP Bound AmbP3==
<StructureSection load='5y72' size='340' side='right'caption='[[5y72]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5y72]] 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=5Y72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y72 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</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=5y72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y72 OCA], [https://pdbe.org/5y72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y72 RCSB], [https://www.ebi.ac.uk/pdbsum/5y72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y72 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/V5TDY7_FISAU V5TDY7_FISAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cyanobacterial prenyltransferase AmbP3 catalyzes the reverse prenylation of the tetracyclic indole alkaloid hapalindole U at its C-2 position. Interestingly, AmbP3 also accepts hapalindole A, a halogenated C-10 epimer of hapalindole U, and catalyzes normal prenylation at its C-2 position. The comparison of the two ternary crystal structures, AmbP3-DMSPP/hapalindole U and AmbP3-DMSPP/hapalindole A, at 1.65-2.00 A resolution revealed two distinct orientations for the substrate binding that define reverse or normal prenylation. The tolerance of the enzyme for these altered orientations is attributed to the hydrophobicity of the substrate binding pocket and the plasticity of the amino acids surrounding the allyl group of the prenyl donor. This is the first study to provide the intimate structural basis for the normal and reverse prenylations catalyzed by a single enzyme, and it offers novel insight into the engineered biosynthesis of prenylated natural products.

Two Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3.,Wong CP, Awakawa T, Nakashima Y, Mori T, Zhu Q, Liu X, Abe I Angew Chem Int Ed Engl. 2018 Jan 8;57(2):560-563. doi: 10.1002/anie.201710682., Epub 2017 Dec 15. PMID:29178634<ref>PMID:29178634</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5y72" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fischerella ambigua UTEX 1903]]
[[Category: Large Structures]]
[[Category: Awakawa T]]
[[Category: Nakashima Y]]
[[Category: Wong CP]]