1YS7
Crystal structure of the response regulator protein prrA complexed with Mg2+
Summary for 1YS7
| Entry DOI | 10.2210/pdb1ys7/pdb |
| Related | 1YS3 1YS6 |
| Descriptor | Transcriptional regulatory protein prrA, MAGNESIUM ION, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | response regulator, dna binding domain, phosphorylation, mycobacterium tuberculosis structural proteomics project, xmtb, structural genomics, transcription regulator |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 2 |
| Total formula weight | 50548.24 |
| Authors | Nowak, E.,Panjikar, S.,Tucker, P.,Mycobacterium Tuberculosis Structural Proteomics Project (XMTB) (deposition date: 2005-02-07, release date: 2006-02-07, Last modification date: 2023-10-25) |
| Primary citation | Nowak, E.,Panjikar, S.,Konarev, P.,Svergun, D.I.,Tucker, P.A. The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis. J.Biol.Chem., 281:9659-9666, 2006 Cited by PubMed Abstract: The structure of the two-domain response regulator PrrA from Mycobacterium tuberculosis shows a compact structure in the crystal with a well defined interdomain interface. The interface, which does not include the interdomain linker, makes the recognition helix and the trans-activation loop of the effector domain inaccessible for interaction with DNA. Part of the interface involves hydrogen-bonding interactions of a tyrosine residue in the receiver domain that is believed to be involved in signal transduction, which, if disrupted, would destabilize the interdomain interface, allowing a more extended conformation of the molecule, which would in turn allow access to the recognition helix. In solution, there is evidence for an equilibrium between compact and extended forms of the protein that is far toward the compact form when the protein is inactivated but moves toward a more extended form when activated by the cognate sensor kinase PrrB. PubMed: 16434396DOI: 10.1074/jbc.M512004200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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