43cq: Difference between revisions
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Created page with "'''Unreleased structure''' The entry 43cq is ON HOLD Authors: Khodi, S. Description: Structure of wild type catalytic domains of E. coli threonine deaminase in complex with PLP Category: Unreleased Structures Category: Khodi, S" |
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==Structure of wild type catalytic domains of E. coli threonine deaminase in complex with PLP== | |||
<StructureSection load='43cq' size='340' side='right'caption='[[43cq]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[43cq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=43CQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=43CQ 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]] 2.9Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | ||
[[Category: Khodi | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=43cq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=43cq OCA], [https://pdbe.org/43cq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=43cq RCSB], [https://www.ebi.ac.uk/pdbsum/43cq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=43cq ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ILVA_ECOLI ILVA_ECOLI] Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.<ref>PMID:13405870</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Khodi S]] | |||
Latest revision as of 19:58, 29 July 2026
Structure of wild type catalytic domains of E. coli threonine deaminase in complex with PLP
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