Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9.

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Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9.

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2017 nî lūn-bûn

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Amino acid residues critical f ...... from Cupriavidus necator NH9.

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Amino acid residues critical f ...... from Cupriavidus necator NH9.

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Amino acid residues critical f ...... from Cupriavidus necator NH9.

@en

Amino acid residues critical f ...... from Cupriavidus necator NH9.

@nl

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Amino acid residues critical f ...... from Cupriavidus necator NH9.

@en

Amino acid residues critical f ...... from Cupriavidus necator NH9.

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P1476

Amino acid residues critical f ...... r from Cupriavidus necator NH9

@en

P2093

Emiko Akiyama

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Jun Shimodaira

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Kaori Takada

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Masae Takabayashi

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Masao Fukuda

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Mayumi Udagawa

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Naoko Kuroda

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Naoto Ogawa

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Ryoichi Minai

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Ryota Moriuchi

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P2860

Structural basis of the redox switch in the OxyR transcription factor

Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend

Distinct effector-binding sites enable synergistic transcriptional activation by BenM, a LysR-type regulator

Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation

The DNA-binding domain of BenM reveals the structural basis for the recognition of a T-N11-A sequence motif by LysR-type transcriptional regulators

The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement

Studies on transformation of Escherichia coli with plasmids

Overlapping binding sites for the virulence gene regulators AphA, AphB and cAMP-CRP at the Vibrio cholerae tcpPH promoter.

Molecular biology of the LysR family of transcriptional regulators

Structural details of the OxyR peroxide-sensing mechanism

P304

2119-2129

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P31

scholarly article

P356

10.1080/09168451.2017.1373592

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P433

http://www.w3.org/2001/XMLSchema#string

P478

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P50

Toshiya Senda

P577

2017-09-22T00:00:00Z

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P698

28936918

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