4q11 | pdb_00004q11

Crystal structure of Proteus mirabilis transcriptional regulator protein Crl at 1.95A resolution

spinqualitylabelsall models 4q11, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q11 is a 2 chain structure with sequence from Proteus mirabilis HI4320. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: NHE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B4EUU9_PROMH Binds to the sigma-S subunit of RNA polymerase, activating expression of sigma-S-regulated genes. Stimulates RNA polymerase holoenzyme formation and may bind to several other sigma factors, such as sigma-70 and sigma-32 (By similarity).[HAMAP-Rule:MF_01178] Publication Abstract from PubMed In many gamma-proteobacteria, the RpoS/sigmaS sigma factor associates with the core RNA polymerase (RNAP) to modify global gene transcription in stationary phase and under stress conditions. The small regulatory protein Crl stimulates the association of sigmaS with the core RNAP in Escherichia coli and Salmonella enterica serovarTyphimurium (S. Typhimurium), through direct and specific interaction with sigmaS. The structural determinants of Crl involved in sigmaS binding are unknown. Here, we report the X-ray crystal structure of the Proteus mirabilis Crl protein (CrlPM) and a structural model for S. 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 sigmaS binding. Among these, charged residues likely to be involved in electrostatic interactions driving Crl-sigmaS complex formation were identified. CrlSTM and CrlPM interact with domain 2 of sigmaS with the same binding properties as with full-length sigmaS. These results suggest that Crl family members share a common mechanism of sigmaS binding in which the flexible arms of Crl might play a dynamic role. Structural and functional features of Crl proteins and identification of conserved surface residues required for interaction with the RpoS/sigmaS subunit of RNA polymerase.,Cavaliere P, Levi-Acobas F, Mayer C, Saul FA, England P, Weber P, Raynal B, Monteil V, Bellalou J, Haouz A, Norel F Biochem J. 2014 Jul 24. PMID:25056110 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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