3o24: Difference between revisions

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 ==Crystal structure of the brevianamide F prenyltransferase FtmPT1 from Aspergillus fumigatus==
-<StructureSection load='3o24' size='340' side='right' caption='[[3o24]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='3o24' size='340' side='right'caption='[[3o24]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3o24]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O24 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O24 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3o24]] is a 1 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=3O24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O24 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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o2k|3o2k]]</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3o24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o24 OCA], [http://pdbe.org/3o24 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o24 RCSB], [http://www.ebi.ac.uk/pdbsum/3o24 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o24 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=3o24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o24 OCA], [https://pdbe.org/3o24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o24 RCSB], [https://www.ebi.ac.uk/pdbsum/3o24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o24 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q4G2I1_ASPFM Q4G2I1_ASPFM]] Catalyzes the prenylation of brevianamide F. Can also prenylate other tryptophan-containing cyclic dipeptides. Prenylation occurs mainly at C-2, but also at C-3.<ref>PMID:16000710</ref> <ref>PMID:23090579</ref>
+[https://www.uniprot.org/uniprot/FTMB_ASPFU FTMB_ASPFU] Brevianamide F prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:16000710, PubMed:23649274). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:19113967, PubMed:21105662, PubMed:23090579). FtmPT1/ftmB shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus (PubMed:18635009). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).<ref>PMID:16000710</ref> <ref>PMID:16755625</ref> <ref>PMID:18635009</ref> <ref>PMID:18683158</ref> <ref>PMID:19113967</ref> <ref>PMID:19226505</ref> <ref>PMID:19763315</ref> <ref>PMID:21105662</ref> <ref>PMID:23090579</ref> <ref>PMID:23649274</ref> <ref>PMID:16000710</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Jost, M]]
+[[Category: Aspergillus fumigatus]]
-[[Category: Stehle, T]]
+[[Category: Large Structures]]
-[[Category: Zocher, G E]]
+[[Category: Jost M]]
-[[Category: Brevianamide f prenyltransferase]]
+[[Category: Stehle T]]
-[[Category: Pt barrel]]
+[[Category: Zocher GE]]
-[[Category: Transferase]]