4ld7
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ld7]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fischeri Aspergillus fischeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ld7]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fischeri Aspergillus fischeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD7 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PIS:TRIHYDROGEN+THIODIPHOSPHATE'>PIS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.83Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PIS:TRIHYDROGEN+THIODIPHOSPHATE'>PIS</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=4ld7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld7 OCA], [https://pdbe.org/4ld7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld7 ProSAT]</span></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=4ld7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld7 OCA], [https://pdbe.org/4ld7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ANAPT_NEOFI ANAPT_NEOFI] Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the prenylated pyrroloindoline diketopiperazine acetylaszonalenin (PubMed:19001367). The first step in the pathway is the formation of (R)-benzodiazepinedione by condensation of tryptophan and anthranilic acid catalyzed by the non-ribosomal peptide synthetase anaPS (PubMed:19001367). The prenyltransferase anaPT then converts (R)-benzodiazepinedione to aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via C3-prenylation (PubMed:19001367, PubMed:19421461, PubMed:20165805, PubMed:24014429, PubMed:26294262). The last step in the biosynthesis of acetylaszonalenin via acetylation of aszonalenin at position N1 catalyzed by anaAT (PubMed:19001367, PubMed:20165805).<ref>PMID:19001367</ref> <ref>PMID:19421461</ref> <ref>PMID:20165805</ref> <ref>PMID:24014429</ref> <ref>PMID:26294262</ref> | [https://www.uniprot.org/uniprot/ANAPT_NEOFI ANAPT_NEOFI] Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the prenylated pyrroloindoline diketopiperazine acetylaszonalenin (PubMed:19001367). The first step in the pathway is the formation of (R)-benzodiazepinedione by condensation of tryptophan and anthranilic acid catalyzed by the non-ribosomal peptide synthetase anaPS (PubMed:19001367). The prenyltransferase anaPT then converts (R)-benzodiazepinedione to aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via C3-prenylation (PubMed:19001367, PubMed:19421461, PubMed:20165805, PubMed:24014429, PubMed:26294262). The last step in the biosynthesis of acetylaszonalenin via acetylation of aszonalenin at position N1 catalyzed by anaAT (PubMed:19001367, PubMed:20165805).<ref>PMID:19001367</ref> <ref>PMID:19421461</ref> <ref>PMID:20165805</ref> <ref>PMID:24014429</ref> <ref>PMID:26294262</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Indole prenyltransferases AnaPT, CdpC3PT, and CdpNPT are known to catalyze the formation of prenylated pyrroloindoline diketopiperazines from tryptophan-containing cyclic dipeptides in one-step reactions. In this study, we investigated the different stereoselectivities of these enzymes toward all the stereoisomers of cyclo-Trp-Ala and cyclo-Trp-Pro. The stereoselectivities of AnaPT and CdpC3PT mainly depend on the configuration of the tryptophanyl moiety in the substrates, and they usually introduce the prenyl moiety from the opposite sides. CdpNPT showed lower stereoselectivity, and the structure of the second amino acid moiety in the substrates is important for the stereospecificity in its enzyme catalysis. Moreover, we determined the crystal structure of AnaPT in complex with thiolodiphosphate and compared it with the known structures of CdpNPT. Our results clearly revealed the presence of an indole binding mode that has so far not been characterized. | ||
| - | + | ==See Also== | |
| - | + | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of AnaPT from Neosartorya fischeri
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