1RZR
crystal structure of transcriptional regulator-phosphoprotein-DNA complex
Summary for 1RZR
Entry DOI | 10.2210/pdb1rzr/pdb |
Descriptor | 5'-D(*CP*TP*GP*AP*AP*AP*GP*CP*GP*CP*TP*AP*AP*CP*AP*G)-3', 5'-D(*CP*TP*GP*TP*TP*AP*GP*CP*GP*CP*TP*TP*TP*CP*AP*G)-3', Glucose-resistance amylase regulator, ... (8 entities in total) |
Functional Keywords | protein-dna complex, phospho-protein, transcription-transport protein-dna complex, transcription/transport protein/dna |
Biological source | Bacillus megaterium More |
Cellular location | Cytoplasm (By similarity): O69250 |
Total number of polymer chains | 12 |
Total formula weight | 205714.17 |
Authors | Schumacher, M.A.,Allen, G.S.,Brennan, R.G. (deposition date: 2003-12-27, release date: 2004-10-12, Last modification date: 2024-10-30) |
Primary citation | Schumacher, M.A.,Allen, G.S.,Diel, M.,Seidel, G.,Hillen, W.,Brennan, R.G. Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell(Cambridge,Mass.), 118:731-741, 2004 Cited by PubMed Abstract: Carbon catabolite repression (CCR) is one of the most fundamental environmental-sensing mechanisms in bacteria and imparts competitive advantage by establishing priorities in carbon metabolism. In gram-positive bacteria, the master transcription regulator of CCR is CcpA. CcpA is a LacI-GalR family member that employs, as an allosteric corepressor, the phosphoprotein HPr-Ser46-P, which is formed in glucose-replete conditions. Here we report structures of the Bacillus megaterium apoCcpA and a CcpA-(HPr-Ser46-P)-DNA complex. These structures reveal that HPr-Ser46-P mediates a novel two-component allosteric DNA binding activation mechanism that involves both rotation of the CcpA subdomains and relocation of pivot-point residue Thr61, which leads to juxtaposition of the DNA binding regions permitting "hinge" helix formation in the presence of cognate DNA. The structure of the CcpA-(HPr-Ser46-P)-cre complex also reveals the elegant mechanism by which CcpA family-specific interactions with HPr-Ser46-P residues Ser46-P and His15 partition the high-energy CCR and low-energy PTS pathways, the latter requiring HPr-His15-P. PubMed: 15369672DOI: 10.1016/j.cell.2004.08.027 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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