View source for 5kcg


==Crystal structure of the aromatic prenyltransferase AtaPT (apo state) from Aspergillus terreus A8-4==
<StructureSection load='5kcg' size='340' side='right'caption='[[5kcg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kcg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_terreus Aspergillus terreus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KCG 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]] 1.9&#8491;</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=5kcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kcg OCA], [https://pdbe.org/5kcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kcg RCSB], [https://www.ebi.ac.uk/pdbsum/5kcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kcg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1B0UHJ4_ASPTE A0A1B0UHJ4_ASPTE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aromatic prenyltransferases (aPTases) transfer prenyl moieties from isoprenoid donors to various aromatic acceptors, some of which have the rare property of extreme enzymatic promiscuity toward both a variety of prenyl donors and a large diversity of acceptors. In this study, we discovered a new aPTase, AtaPT, from Aspergillus terreus that exhibits unprecedented promiscuity toward diverse aromatic acceptors and prenyl donors and also yields products with a range of prenylation patterns. Systematic crystallographic studies revealed various discrete conformations for ligand binding with donor-dependent acceptor specificity and multiple binding sites within a spacious hydrophobic substrate-binding pocket. Further structure-guided mutagenesis of active sites at the substrate-binding pocket is responsible for altering the specificity and promiscuity toward substrates and the diversity of product prenylations. Our study reveals the molecular mechanism underlying the promiscuity of AtaPT and suggests an efficient protein engineering strategy to generate new prenylated derivatives in drug discovery applications.

Molecular insights into the enzyme promiscuity of an aromatic prenyltransferase.,Chen R, Gao B, Liu X, Ruan F, Zhang Y, Lou J, Feng K, Wunsch C, Li SM, Dai J, Sun F Nat Chem Biol. 2017 Feb;13(2):226-234. doi: 10.1038/nchembio.2263. Epub 2016 Dec , 19. PMID:27992881<ref>PMID:27992881</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
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</StructureSection>
[[Category: Aspergillus terreus]]
[[Category: Large Structures]]
[[Category: Gao B]]
[[Category: Sun F]]