1rzr
From Proteopedia
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | CCPA (Bacillus megaterium), PTSH (Bacillus megaterium) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of transcriptional regulator-phosphoprotein-DNA complex
Overview
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.
About this Structure
1RZR is a Protein complex structure of sequences from Bacillus megaterium. Full crystallographic information is available from OCA.
Reference
Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P., Schumacher MA, Allen GS, Diel M, Seidel G, Hillen W, Brennan RG, Cell. 2004 Sep 17;118(6):731-41. PMID:15369672
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