4ld7: Difference between revisions

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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]] 2.83&#8491;</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>  
<div style="background-color:#fffaf0;">
== 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.


Catalytic Mechanism of Stereospecific Formation of cis-Configured Prenylated Pyrroloindoline Diketopiperazines by Indole Prenyltransferases.,Yu X, Zocher G, Xie X, Liebhold M, Schutz S, Stehle T, Li SM Chem Biol. 2013 Nov 12. pii: S1074-5521(13)00364-5. doi:, 10.1016/j.chembiol.2013.10.007. PMID:24239009<ref>PMID:24239009</ref>
==See Also==
 
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ld7" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 15:18, 1 March 2024

Crystal structure of AnaPT from Neosartorya fischeriCrystal structure of AnaPT from Neosartorya fischeri

Structural highlights

4ld7 is a 16 chain structure with sequence from Aspergillus fischeri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.83Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3] [4] [5]

See Also

References

  1. ↑ Yin WB, Grundmann A, Cheng J, Li SM. Acetylaszonalenin biosynthesis in Neosartorya fischeri. Identification of the biosynthetic gene cluster by genomic mining and functional proof of the genes by biochemical investigation. J Biol Chem. 2009 Jan 2;284(1):100-109. doi: 10.1074/jbc.M807606200. Epub 2008 , Nov 10. PMID:19001367 doi:http://dx.doi.org/10.1074/jbc.M807606200
  2. ↑ Yin WB, Cheng J, Li SM. Stereospecific synthesis of aszonalenins by using two recombinant prenyltransferases. Org Biomol Chem. 2009 May 21;7(10):2202-7. doi: 10.1039/b902413a. Epub 2009 Apr , 3. PMID:19421461 doi:http://dx.doi.org/10.1039/b902413a
  3. ↑ Yin WB, Xie XL, Matuschek M, Li SM. Reconstruction of pyrrolo[2,3-b]indoles carrying an alpha-configured reverse C3-dimethylallyl moiety by using recombinant enzymes. Org Biomol Chem. 2010 Mar 7;8(5):1133-41. doi: 10.1039/b922440h. Epub 2010 Jan 7. PMID:20165805 doi:http://dx.doi.org/10.1039/b922440h
  4. ↑ Pockrandt D, Li SM. Geranylation of cyclic dipeptides by the dimethylallyl transferase AnaPT resulting in a shift of prenylation position on the indole ring. Chembiochem. 2013 Oct 11;14(15):2023-8. doi: 10.1002/cbic.201300372. Epub 2013 , Sep 6. PMID:24014429 doi:http://dx.doi.org/10.1002/cbic.201300372
  5. ↑ Zhou K, Yu X, Xie X, Li SM. Complementary Flavonoid Prenylations by Fungal Indole Prenyltransferases. J Nat Prod. 2015 Sep 25;78(9):2229-35. doi: 10.1021/acs.jnatprod.5b00422. Epub , 2015 Aug 21. PMID:26294262 doi:http://dx.doi.org/10.1021/acs.jnatprod.5b00422

4ld7, resolution 2.83Å

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