Format

Send to

Choose Destination
Nat Struct Biol. 2000 Dec;7(12):1139-46.

Novel DNA binding domain and genetic regulation model of Bacillus subtilis transition state regulator abrB.

Author information

1
Department of Chemistry, Purdue University, 1393 Brown Building, West Lafayette, Indiana 47907, USA.

Erratum in

  • Nat Struct Biol. 2005 Apr;12(4):380.

Abstract

We have determined the high resolution NMR solution structure of the novel DNA binding domain of the Bacillus subtilis transition state regulator AbrB. Comparisons of the AbrB DNA binding domain with DNA binding proteins of known structure show that it is a member of a completely novel class of DNA recognition folds that employs a dimeric topology for cellular function. This new DNA binding conformation is referred to as the looped-hinge helix fold. Sequence homology investigations show that this DNA binding topology is found in other disparately related microbes. Structural analysis of the AbrB DNA binding domain together with bioanalytical and mutagenic data of full length AbrB allows us to construct a general model that describes the genetic regulation properties of AbrB.

Comment in

PMID:
11101897
DOI:
10.1038/81999
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center