3HHF
Structure of CrgA regulatory domain, a LysR-type transcriptional regulator from Neisseria meningitidis.
Summary for 3HHF
| Entry DOI | 10.2210/pdb3hhf/pdb |
| Related | 3HHG |
| Descriptor | Transcriptional regulator, LysR family, CHLORIDE ION (3 entities in total) |
| Functional Keywords | neisseria meningitidis, transcription factor, lysr, structural genomics, oxford protein production facility, oppf, dna-binding, transcription, transcription regulation, transcription regulator |
| Biological source | Neisseria meningitidis serogroup B |
| Total number of polymer chains | 2 |
| Total formula weight | 46949.65 |
| Authors | Sainsbury, S.,Ren, J.,Owens, R.J.,Stuart, D.I.,Oxford Protein Production Facility (OPPF) (deposition date: 2009-05-15, release date: 2009-07-07, Last modification date: 2011-07-13) |
| Primary citation | Sainsbury, S.,Lane, L.A.,Ren, J.,Gilbert, R.J.,Saunders, N.J.,Robinson, C.V.,Stuart, D.I.,Owens, R.J. The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators Nucleic Acids Res., 37:4545-4558, 2009 Cited by PubMed Abstract: 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. PubMed: 19474343DOI: 10.1093/nar/gkp445 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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