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A protein structural motif that bends DNA
Author(s) -
White Stephen W.,
Appelt Krzysztof,
Wilson Keith S.,
Tanaka Isao
Publication year - 1989
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340050405
Subject(s) - dna , bacteriophage , escherichia coli , dna binding protein , biology , computational biology , transcription factor , amino acid , structural motif , chemistry , gene , genetics , microbiology and biotechnology , biochemistry
The prokaryotic protein HU, integration host factor (IHF) from Escherichia coli and transcription factor 1 (TF1) from bacteriophage SPO1 are closely related molecules. Biochemical results suggest that the role of these proteins is to bind and bend DNA. From the high‐resolution structure of HU, we propose a model for thisinteraction with DNA. Crucial amino acid differences between the proteins can be rationalized in terms of their different specific functions.

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