1zvv

Crystal structure of a ccpa-crh-dna complex

spinqualitylabelsall models 1zvv, resolution 2.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zvv is a 9 chain structure with sequence from Bacillus subtilis and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.98Å Ligands: IOD, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CCPA_BACSU Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. 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 In Gram-positive bacteria, the catabolite control protein A (CcpA) functions as the master transcriptional regulator of carbon catabolite repression/regulation (CCR). To effect CCR, CcpA binds a phosphoprotein, either HPr-Ser46-P or Crh-Ser46-P. Although Crh and histidine-containing protein (HPr) are structurally homologous, CcpA binds Crh-Ser46-P more weakly than HPr-Ser46-P. Moreover, Crh can form domain-swapped dimers, which have been hypothesized to be functionally relevant in CCR. To understand the molecular mechanism of Crh-Ser46-P regulation of CCR, we determined the structure of a CcpA-(Crh-Ser46-P)-DNA complex. The structure reveals that Crh-Ser46-P does not bind CcpA as a dimer but rather interacts with CcpA as a monomer in a manner similar to that of HPr-Ser46-P. The reduced affinity of Crh-Ser46-P for CcpA as compared with that of HPr-Ser46 P is explained by weaker Crh-Ser46-P interactions in its contact region I to CcpA, which causes this region to shift away from CcpA. Nonetheless, the interface between CcpA and helix alpha 2 of the second contact region (contact region II) of Crh-Ser46-P is maintained. This latter finding demonstrates that this contact region is necessary and sufficient to throw the allosteric switch to activate cre binding by CcpA. Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation.,Schumacher MA, Seidel G, Hillen W, Brennan RG J Biol Chem. 2006 Mar 10;281(10):6793-800. Epub 2005 Nov 29. PMID:16316990 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catabolite control protein 3D structures

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