3ly7

Crystal structure of the periplasmic domain of CadC

spinqualitylabelsall models 3ly7, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ly7 is a 1 chain structure with sequence from Escherichia coli str. K-12 substr. MG1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

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