View source for 4yl7


==Crystal structure of the indole prenyltransferase MpnD from Marinactinospora thermotolerans==
<StructureSection load='4yl7' size='340' side='right'caption='[[4yl7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinactinospora_thermotolerans Marinactinospora thermotolerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YL7 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]] 1.601&#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=4yl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yl7 OCA], [https://pdbe.org/4yl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yl7 RCSB], [https://www.ebi.ac.uk/pdbsum/4yl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yl7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I7EIW6_9ACTN I7EIW6_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prenylation reactions play crucial roles in controlling the activities of biomolecules. Bacterial prenyltransferases, TleC from Streptomyces blastmyceticus and MpnD from Marinactinospora thermotolerans, catalyse the 'reverse' prenylation of (-)-indolactam V at the C-7 position of the indole ring with geranyl pyrophosphate or dimethylallyl pyrophosphate, to produce lyngbyatoxin or pendolmycin, respectively. Using in vitro analyses, here we show that both TleC and MpnD exhibit relaxed substrate specificities and accept various chain lengths (C5-C25) of the prenyl donors. Comparisons of the crystal structures and their ternary complexes with (-)-indolactam V and dimethylallyl S-thiophosphate revealed the intimate structural details of the enzyme-catalysed 'reverse' prenylation reactions and identified the active-site residues governing the selection of the substrates. Furthermore, structure-based enzyme engineering successfully altered the preference for the prenyl chain length of the substrates, as well as the regio- and stereo-selectivities of the prenylation reactions, to produce a series of unnatural novel indolactams.

Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases.,Mori T, Zhang L, Awakawa T, Hoshino S, Okada M, Morita H, Abe I Nat Commun. 2016 Mar 8;7:10849. doi: 10.1038/ncomms10849. PMID:26952246<ref>PMID:26952246</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yl7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Marinactinospora thermotolerans]]
[[Category: Abe I]]
[[Category: Mori T]]
[[Category: Morita H]]