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| | ==Crystal structure of mutant D471N of the periplasmic domain of CadC== | | ==Crystal structure of mutant D471N of the periplasmic domain of CadC== |
| - | <StructureSection load='3ly9' size='340' side='right' caption='[[3ly9]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3ly9' size='340' side='right'caption='[[3ly9]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ly9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LY9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ly9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LY9 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lya|3lya]], [[3ly7|3ly7]], [[3ly8|3ly8]]</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4133, cadC, JW4094 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3ly9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ly9 OCA], [https://pdbe.org/3ly9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ly9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ly9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ly9 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ly9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ly9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ly9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ly9 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CADC_ECOLI CADC_ECOLI]] Required for Pcad induction, a promoter upstream of cadBA that is responsible for the pH-regulated expression of CadA and CadB. Probably acts as an activating transcription factor.<ref>PMID:1370290</ref> | + | [https://www.uniprot.org/uniprot/CADC_ECOLI CADC_ECOLI] Required for Pcad induction, a promoter upstream of cadBA that is responsible for the pH-regulated expression of CadA and CadB. Probably acts as an activating transcription factor.<ref>PMID:1370290</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3ly9" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Transcriptional activator|Transcriptional activator]] | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli str. K-12 substr. MG1655]] |
| - | [[Category: Eichinger, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Skerra, A]] | + | [[Category: Eichinger A]] |
| - | [[Category: Activator]] | + | [[Category: Skerra A]] |
| - | [[Category: Alpha domain]]
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| - | [[Category: Alpha/beta domain]]
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| - | [[Category: Dna-binding]]
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| - | [[Category: Membrane]]
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| - | [[Category: Signaling protein]]
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| - | [[Category: Transcription regulation]]
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| - | [[Category: Transmembrane]]
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| - | [[Category: Two-component regulatory system]]
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| Structural highlights
Function
CADC_ECOLI Required for Pcad induction, a promoter upstream of cadBA that is responsible for the pH-regulated expression of CadA and CadB. Probably acts as an activating transcription factor.[1]
Publication Abstract from PubMed
The membrane-integral transcriptional activator CadC comprises sensory and transcriptional regulatory functions within one polypeptide chain. Its C-terminal periplasmic domain, CadC(pd) , is responsible for sensing of environmental pH as well as for binding of the feedback inhibitor cadaverine. Here we describe the crystal structure of CadC(pd) (residues 188-512) solved at a resolution of 1.8 A via multiple wavelength anomalous dispersion (MAD) using a ReCl(6) (2-) derivative. CadC(pd) reveals a novel fold comprising two subdomains: an N-terminal subdomain dominated by a $\tilde \beta$sheet in contact with three alpha-helices and a C-terminal subdomain formed by a ten-membered alpha-helical bundle, which is oriented almost perpendicular to the helices in the first subdomain. Further to the native protein, crystal structures were also solved for its variants D471N and D471E, which show functionally different behavior in pH sensing. Interestingly, in the heavy metal derivative of CadC(pd) used for MAD phasing a ReCl(6) (2-) ion was found in a cavity located between the two subdomains. Amino acid side chains that coordinate this complex ion are conserved in CadC homologues from various bacterial species, suggesting a function of the cavity in the binding of cadaverine, which was supported by docking studies. Notably, CadC(pd) and its variants form dimers in solution, which can be explained by an extended, albeit rather polar interface between two symmetry-related monomers in the crystal structure. The occurrence of several acidic residues in this region suggests protonation-dependent changes in the mode of dimerization, which could eventually trigger transcriptional activation by CadC in the bacterial cytoplasm.
Crystal structure of the sensory domain of Escherichia coli CadC, a member of the ToxR-like protein family.,Eichinger A, Haneburger I, Koller C, Jung K, Skerra A Protein Sci. 2011 Jan 24. doi: 10.1002/pro.594. PMID:21308846[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Watson N, Dunyak DS, Rosey EL, Slonczewski JL, Olson ER. Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH. J Bacteriol. 1992 Jan;174(2):530-40. PMID:1370290
- ↑ Eichinger A, Haneburger I, Koller C, Jung K, Skerra A. Crystal structure of the sensory domain of Escherichia coli CadC, a member of the ToxR-like protein family. Protein Sci. 2011 Jan 24. doi: 10.1002/pro.594. PMID:21308846 doi:10.1002/pro.594
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