5kvq: Difference between revisions
New page: '''Unreleased structure''' The entry 5kvq is ON HOLD Authors: Meneely, K.M., Lamb, A.L. Description: NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enteroco... |
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The | ==NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocolitica== | ||
<StructureSection load='5kvq' size='340' side='right'caption='[[5kvq]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5kvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KVQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5kvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kvq OCA], [https://pdbe.org/5kvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kvq RCSB], [https://www.ebi.ac.uk/pdbsum/5kvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kvq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O54512_YEREN O54512_YEREN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thiazolinyl imine reductases catalyze the NADPH-dependent reduction of a thiazoline to a thiazolidine, a required step in the formation of the siderophores yersiniabactin (Yersinia spp.) and pyochelin (Pseudomonas aeruginosa). These stand-alone nonribosomal peptide tailoring domains are structural homologues of sugar oxidoreductases. Two closed structures of the thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) are presented here: an NADP+-bound structure to 1.45 A resolution and a holo structure to 1.28 A resolution with NADP+ and a substrate analogue bound. Michaelis-Menten kinetics were measured using the same substrate analogue and the homologue from P. aeruginosa, PchG. The data presented here support the hypothesis that tyrosine 128 is the likely general acid residue for catalysis and also highlight the phosphopantetheine tunnel for tethering of the substrate to the nonribosomal peptide synthetase module during assembly line biosynthesis of the siderophore. | |||
Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.,Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL Biochemistry. 2016 Sep 15. PMID:27601130<ref>PMID:27601130</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Lamb | <div class="pdbe-citations 5kvq" style="background-color:#fffaf0;"></div> | ||
[[Category: Meneely | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Yersinia enterocolitica]] | |||
[[Category: Lamb AL]] | |||
[[Category: Meneely KM]] | |||
Latest revision as of 13:57, 27 September 2023
NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocoliticaNADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocolitica
Structural highlights
FunctionPublication Abstract from PubMedThiazolinyl imine reductases catalyze the NADPH-dependent reduction of a thiazoline to a thiazolidine, a required step in the formation of the siderophores yersiniabactin (Yersinia spp.) and pyochelin (Pseudomonas aeruginosa). These stand-alone nonribosomal peptide tailoring domains are structural homologues of sugar oxidoreductases. Two closed structures of the thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) are presented here: an NADP+-bound structure to 1.45 A resolution and a holo structure to 1.28 A resolution with NADP+ and a substrate analogue bound. Michaelis-Menten kinetics were measured using the same substrate analogue and the homologue from P. aeruginosa, PchG. The data presented here support the hypothesis that tyrosine 128 is the likely general acid residue for catalysis and also highlight the phosphopantetheine tunnel for tethering of the substrate to the nonribosomal peptide synthetase module during assembly line biosynthesis of the siderophore. Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.,Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL Biochemistry. 2016 Sep 15. PMID:27601130[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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