4AB5

Regulatory domain structure of NMB2055 (MetR) a LysR family regulator from N. meningitidis

Summary for 4AB5

• Entry DOI: 10.2210/pdb4ab5/pdb
• Related: 4AB6
• Descriptor: TRANSCRIPTIONAL REGULATOR, LYSR FAMILY (2 entities in total)
• Functional Keywords: transcription factors, transcription
• Biological source: NEISSERIA MENINGITIDIS SEROGROUP B
• Total number of polymer chains: 2
• Total formula weight: 50327.95

Authors

Sainsbury, S.,Ren, J.,Saunders, N.J.,Stuart, D.I.,Owens, R.J. (deposition date: 2011-12-07, release date: 2012-07-11, Last modification date: 2024-10-09)

Primary citation

Sainsbury, S.,Ren, J.,Saunders, N.J.,Stuart, D.I.,Owens, R.J.
Structure of the Regulatory Domain of the Lysr Family Regulator Nmb2055 (Metr-Like Protein) from Neisseria Meningitidis
Acta Crystallogr.,Sect.F, 68:730-, 2012

PubMed Abstract: 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.

PubMed: 22750853
DOI: 10.1107/S1744309112010603

Experimental method

X-RAY DIFFRACTION (2.51 Å)