3bxf: Difference between revisions
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==Crystal structure of effector binding domain of central glycolytic gene regulator (CggR) from Bacillus subtilis in complex with effector fructose-1,6-bisphosphate== | ==Crystal structure of effector binding domain of central glycolytic gene regulator (CggR) from Bacillus subtilis in complex with effector fructose-1,6-bisphosphate== | ||
<StructureSection load='3bxf' size='340' side='right' caption='[[3bxf]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3bxf' size='340' side='right'caption='[[3bxf]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bxf]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3bxf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BXF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</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=3bxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxf OCA], [https://pdbe.org/3bxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxf RCSB], [https://www.ebi.ac.uk/pdbsum/3bxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxf ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CGGR_BACSU CGGR_BACSU] In the absence of glucose, represses the transcription of the gapA operon, which encodes five key glycolytic enzymes. Binds specifically to the cggR-gapA promoter region and blocks the progression of the RNA polymerase, leading to the arrest of the transcription.<ref>PMID:10799476</ref> <ref>PMID:12622823</ref> <ref>PMID:20462860</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 37: | Line 36: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Otwinowski Z]] | ||
[[Category: | [[Category: Rezacova P]] | ||
Latest revision as of 15:18, 30 August 2023
Crystal structure of effector binding domain of central glycolytic gene regulator (CggR) from Bacillus subtilis in complex with effector fructose-1,6-bisphosphateCrystal structure of effector binding domain of central glycolytic gene regulator (CggR) from Bacillus subtilis in complex with effector fructose-1,6-bisphosphate
Structural highlights
FunctionCGGR_BACSU In the absence of glucose, represses the transcription of the gapA operon, which encodes five key glycolytic enzymes. Binds specifically to the cggR-gapA promoter region and blocks the progression of the RNA polymerase, leading to the arrest of the transcription.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedExpression of genes in the gapA operon encoding five enzymes for triose phosphate interconversion in Bacillus subtilis is negatively regulated by the Central glycolytic genes Regulator (CggR). CggR belongs to the large SorC/DeoR family of prokaryotic transcriptional regulators, characterized by an N-terminal DNA-binding domain and a large C-terminal effector-binding domain. When no glucose is present in growth media, CggR binds to its target DNA sequence and blocks the transcription of genes in the gapA operon. In the presence of glucose, binding of the known effector molecule fructose-1,6-bisphosphate abolishes this interaction. We have identified dihydroxyacetone phosphate, glucose-6-phosphate, and fructose-6-phosphate as additional CggR ligands that can bind to the effector-binding site. Crystal structures of C-CggR, the C-terminal effector-binding domain of CggR, both unliganded as well as in complex with the four ligands at resolutions between 1.65 and 1.80 A reveal unique ligand-specific structural changes in the binding site that affect the dimer interface. Binding affinities of these ligands were determined by isothermal titration calorimetry. Chemical cross-linking shows that CggR oligomerization is mediated through its effector-binding domain and that binding of the different ligands differentially affects the distribution of oligomers. Electrophoretic mobility shift assays (EMSAs) confirmed a destabilizing effect of FBP on the CggR/DNA complex and also showed similar effects for dihydroxyacetone phosphate. Our results suggest that CggR stability and function may be modulated by various effectors in a complex fashion. Crystal structures of the effector-binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates.,Rezacova P, Kozisek M, Moy SF, Sieglova I, Joachimiak A, Machius M, Otwinowski Z Mol Microbiol. 2008 Jun 10;. PMID:18554327[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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