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| | ==Crystal structure of CdpNPT in its unbound state== | | ==Crystal structure of CdpNPT in its unbound state== |
| - | <StructureSection load='4e0t' size='340' side='right' caption='[[4e0t]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='4e0t' size='340' side='right'caption='[[4e0t]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4e0t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E0T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4e0t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E0T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e0u|4e0u]]</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=4e0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0t OCA], [https://pdbe.org/4e0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e0t RCSB], [https://www.ebi.ac.uk/pdbsum/4e0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e0t ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cdpNPT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])</td></tr>
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| - | <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=4e0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0t OCA], [http://pdbe.org/4e0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e0t RCSB], [http://www.ebi.ac.uk/pdbsum/4e0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e0t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/D1D8L6_ASPFM D1D8L6_ASPFM]] |
| | <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: Aspfm]] | + | [[Category: Aspergillus fumigatus]] |
| - | [[Category: Schuller, J M]] | + | [[Category: Large Structures]] |
| - | [[Category: Stehle, T]] | + | [[Category: Schuller JM]] |
| - | [[Category: Zocher, G]] | + | [[Category: Stehle T]] |
| - | [[Category: Pt-fold]] | + | [[Category: Zocher G]] |
| - | [[Category: Transferase]]
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| Structural highlights
Function
[D1D8L6_ASPFM]
Publication Abstract from PubMed
Fungal indole prenyltransferases (PTs) typically act on specific substrates, and they are able to prenylate their target compounds with remarkably high regio- and stereoselectivity. Similar to several indole PTs characterized to date, the cyclic dipeptide N-prenyltransferase (CdpNPT) is able to prenylate a range of diverse substrates, thus exhibiting an unusually broad substrate promiscuity. To define the structural basis for this promiscuity, we have determined crystal structures of unliganded CdpNPT and of a ternary complex of CdpNPT bound to (S)-benzodiazepinedione and thiolodiphosphate. Analysis of the structures reveals a limited number of specific interactions with (S)-benzodiazepinedione, which projects into a largely hydrophobic surface. This surface can also accommodate other substrates, explaining the ability of the enzyme to prenylate a range of compounds. The location of the bound substrates suggests a likely reaction mechanism for the conversion of (S)-benzodiazepinedione. Structure-guided mutagenesis experiments confirm that, in addition to (S)-benzodiazepinedione, CdpNPT can also act on (R)-benzodiazepinedione and several cyclic dipeptides, albeit with relaxed specificity. Finally, nuclear magnetic resonance spectroscopy demonstrates that CdpNPT is a C-3 reverse PT that catalyzes the formation of C-3beta prenylated indolines from diketopiperazines of tryptophan-containing cyclic dipeptides.
Structure and catalytic mechanism of a cyclic dipeptide prenyltransferase with broad substrate promiscuity.,Schuller JM, Zocher G, Liebhold M, Xie X, Stahl M, Li SM, Stehle T J Mol Biol. 2012 Sep 7;422(1):87-99. Epub 2012 Jun 6. PMID:22683356[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schuller JM, Zocher G, Liebhold M, Xie X, Stahl M, Li SM, Stehle T. Structure and catalytic mechanism of a cyclic dipeptide prenyltransferase with broad substrate promiscuity. J Mol Biol. 2012 Sep 7;422(1):87-99. Epub 2012 Jun 6. PMID:22683356 doi:10.1016/j.jmb.2012.05.033
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