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

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 cyste...

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Publication status:
Published

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Publisher copy:
10.1107/s1744309112010603

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Volume:
68
Issue:
Pt 7
Pages:
730-737
Publication date:
2012-07-05
DOI:
EISSN:
1744-3091
ISSN:
1744-3091
URN:
uuid:413b1bdb-0cca-4282-9c90-6bdd04d4d0d9
Source identifiers:
341066
Local pid:
pubs:341066

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