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Structural basis for DNA recognition by the transcription regulator MetR.

Abstract:

MetR, a LysR-type transcriptional regulator (LTTR), has been extensively studied owing to its role in the control of methionine biosynthesis in proteobacteria. A MetR homodimer binds to a 24-base-pair operator region of the met genes and specifically recognizes the interrupted palindromic sequence 5'-TGAA-N5-TTCA-3'. Mechanistic details underlying the interaction of MetR with its target DNA at the molecular level remain unknown. In this work, the crystal structure of the DNA-binding domain (D...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1107/S2053230X16006828

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Publisher:
International Union of Crystallography Publisher's website
Journal:
Acta Crystallographica Section F: Structural Biology Communications Journal website
Volume:
72
Issue:
Pt 6
Pages:
417-426
Publication date:
2016-05-23
DOI:
EISSN:
2053-230X
URN:
uuid:36134a27-f8c5-4be4-a4b6-250981e81503
Source identifiers:
628905
Local pid:
pubs:628905

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