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{{Large structure}} | {{Large structure}} | ||
==Crystal structure of AnaPT from Neosartorya fischeri== | |||
=== | <StructureSection load='4ld7' size='340' side='right' caption='[[4ld7]], [[Resolution|resolution]] 2.83Å' scene=''> | ||
{{ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ld7]] is a 16 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LD7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PIS:TRIHYDROGEN+THIODIPHOSPHATE'>PIS</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NFIA_055300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36630 Aspergillus fischeri])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-dimethylallyltryptophan_synthase 4-dimethylallyltryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.34 2.5.1.34] </span></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=4ld7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld7 OCA], [http://pdbe.org/4ld7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ld7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ld7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld7 ProSAT]</span></td></tr> | |||
</table> | |||
{{Large structure}} | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
<div class="pdbe-citations 4ld7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: 4-dimethylallyltryptophan synthase]] | [[Category: 4-dimethylallyltryptophan synthase]] | ||
[[Category: Stehle, T | [[Category: Aspergillus fischeri]] | ||
[[Category: Zocher, G | [[Category: Stehle, T]] | ||
[[Category: Zocher, G]] | |||
[[Category: Abba-prenyltransferase]] | [[Category: Abba-prenyltransferase]] | ||
[[Category: Prenyltransferase]] | [[Category: Prenyltransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 06:13, 5 August 2016
Warning: this is a large structure, and loading might take a long time or not happen at all.
Crystal structure of AnaPT from Neosartorya fischeriCrystal structure of AnaPT from Neosartorya fischeri
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMedIndole 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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