3hhf | pdb_00003hhf

Structure of CrgA regulatory domain, a LysR-type transcriptional regulator from Neisseria meningitidis.

spinqualitylabelsall models 3hhf, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hhf is a 2 chain structure with sequence from Neisseria meningitidis serogroup B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CRGA_NEIMB Regulatory protein that activates transcription of mdaB, encoding a NADPH:quinone oxidoreductase, and represses its own transcription (PubMed:15866928). Under the same experimental conditions, no regulation of transcription of pilus and capsule genes is detected (PubMed:15866928). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed LysR-type transcriptional regulators (LTTRs) form the largest family of bacterial regulators acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes. The LTTR, CrgA, from the human pathogen Neisseria meningitidis, is upregulated during bacterial-host cell contact. Here, we report the crystal structures of both regulatory domain and full-length CrgA, the first of a novel subclass of LTTRs that form octameric rings. Non-denaturing mass spectrometry analysis and analytical ultracentrifugation established that the octameric form of CrgA is the predominant species in solution in both the presence and absence of an oligonucleotide encompassing the CrgA-binding sequence. Furthermore, analysis of the isolated CrgA-DNA complex by mass spectrometry showed stabilization of a double octamer species upon DNA binding. Based on the observed structure and the mass spectrometry findings, a model is proposed in which a hexadecameric array of two CrgA oligomers binds to its DNA target site. The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators.,Sainsbury S, Lane LA, Ren J, Gilbert RJ, Saunders NJ, Robinson CV, Stuart DI, Owens RJ Nucleic Acids Res. 2009 Aug;37(14):4545-58. Epub 2009 May 27. PMID:19474343 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

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