1ZVV
Crystal structure of a ccpa-crh-dna complex
Summary for 1ZVV
| Entry DOI | 10.2210/pdb1zvv/pdb |
| Related | 1RZR 1SXG 1SXH 1SXI |
| Descriptor | DNA recognition strand CRE, Glucose-resistance amylase regulator, HPr-like protein crh, ... (5 entities in total) |
| Functional Keywords | ccpa; crh; dna; complex; laci member, transcription-dna complex, transcription/dna |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 9 |
| Total formula weight | 154508.62 |
| Authors | Schumacher, M.A.,Brennan, R.G.,Hillen, W.,Seidel, G. (deposition date: 2005-06-02, release date: 2006-02-07, Last modification date: 2024-11-20) |
| Primary citation | Schumacher, M.A.,Seidel, G.,Hillen, W.,Brennan, R.G. Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation. J.Biol.Chem., 281:6793-6800, 2006 Cited by PubMed Abstract: 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. PubMed: 16316990DOI: 10.1074/jbc.M509977200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.98 Å) |
Structure validation
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