4Q11
Crystal structure of Proteus mirabilis transcriptional regulator protein Crl at 1.95A resolution
Summary for 4Q11
| Entry DOI | 10.2210/pdb4q11/pdb |
| Related | 3RPJ |
| Descriptor | Sigma factor-binding protein Crl, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total) |
| Functional Keywords | transcription regulator, sigma factor |
| Biological source | Proteus mirabilis |
| Cellular location | Cytoplasm (By similarity): B4EUU9 |
| Total number of polymer chains | 2 |
| Total formula weight | 31942.82 |
| Authors | Norel, F.,Mayer, C.,Saul, F.A.,Haouz, A. (deposition date: 2014-04-02, release date: 2014-08-06, Last modification date: 2023-09-20) |
| Primary citation | Cavaliere, P.,Levi-Acobas, F.,Mayer, C.,Saul, F.A.,England, P.,Weber, P.,Raynal, B.,Monteil, V.,Bellalou, J.,Haouz, A.,Norel, F. Structural and functional features of Crl proteins and identification of conserved surface residues required for interaction with the RpoS/ sigma S subunit of RNA polymerase. Biochem.J., 463:215-224, 2014 Cited by PubMed Abstract: In many γ-proteobacteria, the RpoS/σS sigma factor associates with the core RNAP (RNA polymerase) to modify global gene transcription in stationary phase and under stress conditions. The small regulatory protein Crl stimulates the association of σS with the core RNAP in Escherichia coli and Salmonella enterica serovar Typhimurium, through direct and specific interaction with σS. The structural determinants of Crl involved in σS binding are unknown. In the present paper we report the X-ray crystal structure of the Proteus mirabilis Crl protein (CrlPM) and a structural model for Salmonella Typhimurium Crl (CrlSTM). Using a combination of in vivo and in vitro assays, we demonstrated that CrlSTM and CrlPM are structurally similar and perform the same biological function. In the Crl structure, a cavity enclosed by flexible arms contains two patches of conserved and exposed residues required for σS binding. Among these, charged residues that are likely to be involved in electrostatic interactions driving Crl-σS complex formation were identified. CrlSTM and CrlPM interact with domain 2 of σS with the same binding properties as with full-length σS. These results suggest that Crl family members share a common mechanism of σS binding in which the flexible arms of Crl might play a dynamic role. PubMed: 25056110DOI: 10.1042/BJ20140578 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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