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| | <StructureSection load='4yzk' size='340' side='right'caption='[[4yzk]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='4yzk' size='340' side='right'caption='[[4yzk]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yzk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_blastmyceticus"_watanabe_et_al._1957 "streptomyces blastmyceticus" watanabe et al. 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YZK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yzk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_blastmyceticus Streptomyces blastmyceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YZK FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yzj|4yzj]], [[4yzl|4yzl]]</td></tr> | + | </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=4yzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzk OCA], [https://pdbe.org/4yzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yzk RCSB], [https://www.ebi.ac.uk/pdbsum/4yzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzk ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tleC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68180 "Streptomyces blastmyceticus" Watanabe et al. 1957])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzk OCA], [http://pdbe.org/4yzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yzk RCSB], [http://www.ebi.ac.uk/pdbsum/4yzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A077K887_9ACTN A0A077K887_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces blastmyceticus watanabe et al. 1957]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abe, I]] | + | [[Category: Streptomyces blastmyceticus]] |
| - | [[Category: Mori, T]] | + | [[Category: Abe I]] |
| - | [[Category: Morita, H]] | + | [[Category: Mori T]] |
| - | [[Category: Indolactam v]] | + | [[Category: Morita H]] |
| - | [[Category: Indole prenyltransferase]]
| + | |
| - | [[Category: Pt-fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A0A077K887_9ACTN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mori T, Zhang L, Awakawa T, Hoshino S, Okada M, Morita H, Abe I. Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases. Nat Commun. 2016 Mar 8;7:10849. doi: 10.1038/ncomms10849. PMID:26952246 doi:http://dx.doi.org/10.1038/ncomms10849
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