Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) from Neisseria meningitidis

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 68; no. 7; pp. 730 - 737
• Main Authors: Sainsbury, Sarah, Ren, Jingshan, Saunders, Nigel J., Stuart, David I., Owens, Raymond J.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.07.2012
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bonding; Crystal structure; Cysteine; Disulfides; Disulfides - chemistry; Disulfides - metabolism; LysR-type regulator; MetR; Models, Molecular; Molecular Sequence Data; Mutation; Mutations; Neisseria meningitidis; Neisseria meningitidis - chemistry; Neisseria meningitidis - metabolism; Pocket; Protein Structure, Quaternary; Protein Structure, Tertiary; Regulators; Residues; Sequence Alignment; Structural Communications; Structural Homology, Protein; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309112010603

The crystal structure of the regulatory domain of NMB2055, a putative MetR regulator from Neisseria meningitidis, is reported at 2.5 Å resolution. The structure revealed that there is a disulfide bond inside the predicted effector‐binding pocket of the regulatory domain. Mutation of the cysteines (Cys103 and Cys106) that form the disulfide bond to serines resulted in significant changes to the structure of the effector pocket. Taken together with the high degree of conservation of these cysteine residues within MetR‐related transcription factors, it is suggested that the Cys103 and Cys106 residues play an important role in the function of MetR regulators.