View source for 9jhx


==Versatile Aromatic Prenyltransferase auraA mutant-Y207A in complex with DMSPP==
<StructureSection load='9jhx' size='340' side='right'caption='[[9jhx]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jhx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_solitum Penicillium solitum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JHX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.86&#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=9jhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jhx OCA], [https://pdbe.org/9jhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jhx RCSB], [https://www.ebi.ac.uk/pdbsum/9jhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jhx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prenylation modifications of natural products play essential roles in chemical diversity and bioactivities, but imidazole modification prenyltransferases are not well investigated. Here, we discover a dimethylallyl tryptophan synthase family prenyltransferase, AuraA, that catalyzes the rare dimethylallylation on the imidazole moiety in the biosynthesis of aurantiamine. Biochemical assays validate that AuraA could accept both cyclo-(L-Val-L-His) and cyclo-(L-Val-DH-His) as substrates, while the prenylation modes are completely different, yielding C2-regular and C5-reverse products, respectively. Cryo-electron microscopy analysis of AuraA and its two ternary complex structures reveal two distinct modes for receptor binding, demonstrating a tolerance for altered orientations of highly similar receptors. The mutation experiments further demonstrate the promiscuity of AuraA towards imidazole-C-dimethylallylation. In this work, we also characterize a case of AuraA mutant-catalyzed dimethylallylation of imidazole moiety, offering available structural insights into the utilization and engineering of dimethylallyl tryptophan synthase family prenyltransferases.

Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines.,Wang W, Wang P, Ma C, Li K, Wang Z, Liu Y, Wang L, Zhang G, Che Q, Zhu T, Zhang Y, Li D Nat Commun. 2025 Jan 2;16(1):144. doi: 10.1038/s41467-024-55537-8. PMID:39747040<ref>PMID:39747040</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9jhx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Penicillium solitum]]
[[Category: Li D]]
[[Category: Wang P]]
[[Category: Wang W]]
[[Category: Zhang Y]]