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| | <StructureSection load='2fyi' size='340' side='right'caption='[[2fyi]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2fyi' size='340' side='right'caption='[[2fyi]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fyi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fyi]] is a 4 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=2FYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYI FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbl ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=2fyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyi OCA], [https://pdbe.org/2fyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyi RCSB], [https://www.ebi.ac.uk/pdbsum/2fyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyi ProSAT]</span></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=2fyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyi OCA], [https://pdbe.org/2fyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyi RCSB], [https://www.ebi.ac.uk/pdbsum/2fyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CBL_ECOLI CBL_ECOLI]] May be an accessory regulatory protein within the cys regulon.
| + | [https://www.uniprot.org/uniprot/CBL_ECOLI CBL_ECOLI] May be an accessory regulatory protein within the cys regulon. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brzozowski, A M]] | + | [[Category: Brzozowski AM]] |
| - | [[Category: Bujacz, G D]] | + | [[Category: Bujacz GD]] |
| - | [[Category: Neumann, P]] | + | [[Category: Neumann P]] |
| - | [[Category: Stec, E]] | + | [[Category: Stec E]] |
| - | [[Category: Wilkinson, A J]] | + | [[Category: Wilkinson AJ]] |
| - | [[Category: Cofactor-binding domain]]
| + | |
| - | [[Category: Cysteine biosynthesis]]
| + | |
| - | [[Category: Lys-r family]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcriptional regulator]]
| + | |
| Structural highlights
Function
CBL_ECOLI May be an accessory regulatory protein within the cys regulon.
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 PubMed
Cbl is a member of the large family of LysR-type transcriptional regulators (LTTRs) common in bacteria and found also in Archaea and algal chloroplasts. The function of Cbl is required in Escherichia coli for expression of sulphate starvation-inducible (ssi) genes, associated with the biosynthesis of cysteine from organic sulphur sources (sulphonates). Here, we report the crystal structure of the cofactor-binding domain of Cbl (c-Cbl) from E. coli. The overall fold of c-Cbl is very similar to the regulatory domain (RD) of another LysR family member, CysB. The RD is composed of two subdomains enclosing a cavity, which is expected to bind effector molecules. We have constructed and analysed several full-length Cbl variants bearing single residue substitutions in the RD that affect cofactor responses. Using in vivo and in vitro transcription assays, we demonstrate that pssuE, a Cbl responsive promoter, is down-regulated not only by the cofactor, adenosine phosphosulphate (APS), but also by thiosulphate, and, that the same RD determinants are important for the response to both cofactors. We also demonstrate the effects of selected site-directed mutations on Cbl oligomerization and discuss these in the context of the structure. Based on the crystal structure and molecular modelling, we propose a model for the interaction of Cbl with adenosine phosphosulphate.
Structural basis of the sulphate starvation response in E. coli: crystal structure and mutational analysis of the cofactor-binding domain of the Cbl transcriptional regulator.,Stec E, Witkowska-Zimny M, Hryniewicz MM, Neumann P, Wilkinson AJ, Brzozowski AM, Verma CS, Zaim J, Wysocki S, Bujacz GD J Mol Biol. 2006 Dec 1;364(3):309-22. Epub 2006 Jun 30. PMID:17010379[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stec E, Witkowska-Zimny M, Hryniewicz MM, Neumann P, Wilkinson AJ, Brzozowski AM, Verma CS, Zaim J, Wysocki S, Bujacz GD. Structural basis of the sulphate starvation response in E. coli: crystal structure and mutational analysis of the cofactor-binding domain of the Cbl transcriptional regulator. J Mol Biol. 2006 Dec 1;364(3):309-22. Epub 2006 Jun 30. PMID:17010379 doi:10.1016/j.jmb.2006.06.033
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