The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators.

Journal article

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....

Expand abstract

Authors: Sainsbury, S; Lane, L; Ren, J; Gilbert, R; Saunders, N

• Publication status: Published
• Journal: Nucleic acids research
• Volume: 37
• Issue: 14
• Pages: 4545-4558
• Publication date: 2009-08-01
• DOI: 10.1093/nar/gkp445
• EISSN: 1362-4962
• ISSN: 0305-1048
• Language: English
• Keywords: DNA; Molecular Sequence Data; Transcription Factors; Crystallography, X-Ray; Bacterial Proteins; Protein Structure, Tertiary; Ultracentrifugation; Protein Multimerization; Binding Sites; Mass Spectrometry; Amino Acid Sequence; Models, Molecular