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Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/6672

Title: Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) from Neisseria meningitidis
Authors: Sainsbury, S
Ren, J
Saunders, NJ
Stuart, DI
Owens, RJ
Keywords: MetR
Neisseria meningitidis
LysR-type regulator
Publication Date: 2012
Publisher: International Union of Crystallography
Citation: Acta Crystallographica Section F, 68(7): 730 - 737, Jul 2012
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.
Description: Copyright @ 2012 International Union of Crystallography
Sponsorship: This study is funded by the Medical Research Council, with additional finance from the Biotechnology and Biological Science Research Council.
URI: http://onlinelibrary.wiley.com/doi/10.1107/S1744309112010603/abstract
http://bura.brunel.ac.uk/handle/2438/6672
DOI: http://dx.doi.org/10.1107/S1744309112010603
ISSN: 1744-3091
Appears in Collections:School of Health Sciences and Social Care Research Papers
Biosciences
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