Journal article icon

Journal article

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...

Expand abstract

Actions


Access Document


Publisher copy:
10.1107/S1744309112010603

Authors


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:
7
Pages:
730-737
Publication date:
2012-07-05
DOI:
EISSN:
1744-3091
URN:
uuid:7d05e151-bd58-4829-a647-2ac60ccc88ed
Source identifiers:
342873
Local pid:
pubs:342873
Language:
English
Keywords:

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP