View source for 9iia


==Crystal structure of the free histidine prenyltransferase FunA==
<StructureSection load='9iia' size='340' side='right'caption='[[9iia]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9iia]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_tricinctum Fusarium tricinctum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IIA 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]] 2.27&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MOE:METHOXY-ETHOXYL'>MOE</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene>, <scene name='pdbligand=TOE:2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL'>TOE</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=9iia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9iia OCA], [https://pdbe.org/9iia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9iia RCSB], [https://www.ebi.ac.uk/pdbsum/9iia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9iia ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A8K0WD55_9HYPO A0A8K0WD55_9HYPO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prenylation of amino acids is a critical step for synthesizing building blocks of prenylated alkaloid family natural products, where the corresponding prenyltransferase that catalyzes prenylation on free l-histidine (l-His) has not yet been identified. Here, we first discovered and characterized a prenyltransferase FunA from the antifungal agent fungerin pathway that efficiently performs C4-dimethylallylation on l-His. Crystal structure-guided engineering of the prenyl-binding pocket of FunA, a single M181A mutation, successfully converted it into a C4-geranyltransferase. Furthermore, FunA and its variant FunA-M181A show broad substrate promiscuity toward substrates that vary in substituents of the imidazole ring. Our work furthers our knowledge of free amino acid prenyltransferase and expands the arsenal of alkylation biocatalysts for imidazole-containing small molecules.

Discovery, Characterization and Engineering of the Free l-Histidine C4-Prenyltransferase.,Chen XW, Liu Z, Dai S, Zou Y J Am Chem Soc. 2024 Aug 28;146(34):23686-23691. doi: 10.1021/jacs.4c08388. Epub , 2024 Aug 14. PMID:39140691<ref>PMID:39140691</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9iia" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fusarium tricinctum]]
[[Category: Large Structures]]
[[Category: Chen X]]
[[Category: Dai S]]
[[Category: Liu Z]]
[[Category: Zou Y]]