View source for 6pgn


==PagF single mutant with GPP==
<StructureSection load='6pgn' size='340' side='right'caption='[[6pgn]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pgn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Planktothrix_agardhii Planktothrix agardhii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PGN 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPP:GERANYL+DIPHOSPHATE'>GPP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6pgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pgn OCA], [https://pdbe.org/6pgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pgn RCSB], [https://www.ebi.ac.uk/pdbsum/6pgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pgn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1J1JDI6_PLAAG A0A1J1JDI6_PLAAG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mutation at a single amino acid alters the isoprene donor specificity of prenyltransferases involved in the modification of ribosomally synthesized and post-translationally modified peptides (RiPPs). Though most characterized RiPP prenyltransferases carry out the regiospecific transfer of C5 dimethylallyl donor to the side chain atoms on macrocyclic acceptor substrates, the elucidation of the cyanobactin natural product piricyclamide 70005E1 identifies an O-geranyl modification on Tyr, a reaction with little prior biochemical precedence. Reconstitution and kinetic studies of the presumptive geranyltransferase PirF shows that the enzyme utilizes a C10 donor, with no C5 transferase activity. The crystal structure of PirF reveals a single amino acid difference in the vicinity of the isoprene-binding pocket, relative to the C5 utilizing enzymes. Remarkably, only a single amino acid mutation is necessary to completely switch the donor specificity from a C5 to a C10 prenyltransferase, and vice versa. Lastly, we demonstrate that these enzymes may be used for the chemospecific attachment of C5 or C10 lipid groups on lanthipeptides, an unrelated class of RiPP natural products. These studies represent a rare example where prenyl donor specificity can be discretely altered, which expands the arsenal of synthetic biology tools for tuning biological activities of peptide natural products.

A Single Amino Acid Switch Alters the Isoprene Donor Specificity in Ribosomally Synthesized and Post-Translationally Modified Peptide Prenyltransferases.,Estrada P, Morita M, Hao Y, Schmidt EW, Nair SK J Am Chem Soc. 2018 Jul 5;140(26):8124-8127. doi: 10.1021/jacs.8b05187. Epub 2018, Jun 26. PMID:29924593<ref>PMID:29924593</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pgn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Planktothrix agardhii]]
[[Category: Estrada P]]
[[Category: Hao Y]]
[[Category: Nair SK]]