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PMID: 6540370 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

3-A resolution structure of a protein with histone-like properties in prokaryotes.

Nature ·Vol. 310 ·No. 5976 ·1984-00-00 ·Pages 376-81

Tanaka I, Appelt K, Dijk J, White SW, Wilson KS

Abstract

The 3-A structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined. The molecule is dimeric and appears to bind to the phosphate backbone of DNA through two symmetry-related arms. A mechanism by which the protein induces DNA supercoiling is proposed.

MeSH Terms
Amino Acid Sequence Bacterial Proteins DNA, Superhelical DNA-Binding Proteins Geobacillus stearothermophilus Histones Macromolecular Substances Protein Binding Protein Conformation
Chemicals
Bacterial Proteins DNA, Superhelical DNA-Binding Proteins Histones Macromolecular Substances
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Tanaka I
Appelt K
Dijk J
White S W
Wilson K S
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/310376a0
Published
1984-00-00
Pages
376-81
Language
English
Region
England
NLM ID
0410462
Subset
IM
External Links
PubMed source DOI: 10.1038/310376a0 View journal details
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