5t4l: Difference between revisions
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<StructureSection load='5t4l' size='340' side='right'caption='[[5t4l]], [[Resolution|resolution]] 1.53Å' scene=''> | <StructureSection load='5t4l' size='340' side='right'caption='[[5t4l]], [[Resolution|resolution]] 1.53Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5t4l]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5t4l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T4L FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=77E:(4R)-4-AMINO-6-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}HEXANOIC+ACID'>77E</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=5t4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t4l OCA], [https://pdbe.org/5t4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t4l RCSB], [https://www.ebi.ac.uk/pdbsum/5t4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t4l ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | *[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | ||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Belitsky | [[Category: Belitsky BR]] | ||
[[Category: Farley | [[Category: Farley M]] | ||
[[Category: Juncosa | [[Category: Juncosa JI]] | ||
[[Category: Le | [[Category: Le HV]] | ||
[[Category: Lehrer | [[Category: Lehrer HJS]] | ||
[[Category: Liu | [[Category: Liu D]] | ||
[[Category: Petsko | [[Category: Petsko GA]] | ||
[[Category: Ringe | [[Category: Ringe D]] | ||
[[Category: Sanishvili | [[Category: Sanishvili R]] | ||
[[Category: Silverman | [[Category: Silverman RB]] | ||
[[Category: Wu | [[Category: Wu R]] | ||
Latest revision as of 15:54, 4 October 2023
PLP and GABA Trigger GabR-Mediated Transcription Regulation in Bacillus subsidies via External Aldimine FormationPLP and GABA Trigger GabR-Mediated Transcription Regulation in Bacillus subsidies via External Aldimine Formation
Structural highlights
FunctionPublication Abstract from PubMedThe Bacillus subtilis protein regulator of the gabTD operon and its own gene (GabR) is a transcriptional activator that regulates transcription of gamma-aminobutyric acid aminotransferase (GABA-AT; GabT) upon interactions with pyridoxal-5'-phosphate (PLP) and GABA, and thereby promotes the biosynthesis of glutamate from GABA. We show here that the external aldimine formed between PLP and GABA is apparently responsible for triggering the GabR-mediated transcription activation. Details of the "active site" in the structure of the GabR effector-binding/oligomerization (Eb/O) domain suggest that binding a monocarboxylic gamma-amino acid such as GABA should be preferred over dicarboxylic acid ligands. A reactive GABA analog, (S)-4-amino-5-fluoropentanoic acid (AFPA), was used as a molecular probe to examine the reactivity of PLP in both GabR and a homologous aspartate aminotransferase (Asp-AT) from Escherichia coli as a control. A comparison between the structures of the Eb/O-PLP-AFPA complex and Asp-AT-PLP-AFPA complex revealed that GabR is incapable of facilitating further steps of the transamination reaction after the formation of the external aldimine. Results of in vitro and in vivo assays using full-length GabR support the conclusion that AFPA is an agonistic ligand capable of triggering GabR-mediated transcription activation via formation of an external aldimine with PLP. PLP and GABA trigger GabR-mediated transcription regulation in Bacillus subtilis via external aldimine formation.,Wu R, Sanishvili R, Belitsky BR, Juncosa JI, Le HV, Lehrer HJ, Farley M, Silverman RB, Petsko GA, Ringe D, Liu D Proc Natl Acad Sci U S A. 2017 Mar 27. pii: 201703019. doi:, 10.1073/pnas.1703019114. PMID:28348215[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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