The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases

Journal of Molecular Biology

Volumn 324, Issue 2, 2002, Pages 227-236

  Cheng, Yi Sheng ^a   Hsia, Kuo Chiang ^a   Doudeva, Lyudmila G ^a   Chak, Kin Fu ^b   Yuan, Hanna S ^a  

^a INSTITUTE OF MOLECULAR BIOLOGY   (Taiwan)

^b NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

Colicin; DNA binding; Endonuclease structure; H N H motif; Zn enzyme

Indexed keywords

BACTERIAL TOXIN; COLICIN E7; DIMER; DOUBLE STRANDED DNA; ENDONUCLEASE; NUCLEASE; PROTEIN; PROTEIN IM7; RNA; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; BINDING KINETICS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CROSS LINKING; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN BINDING; STRUCTURAL HOMOLOGY;

BACTERIA (MICROORGANISMS);

EID: 0036440979     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01092-6     Document Type: Article

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