Autor:	Mark A. Strauch, Jeffrey L. Vaughn, Victoria A. Feher, Stephen Naylor, John Cavanagh
Rok vydání:	2000
Předmět:	Genetics HMG-box Base pair fungi DNA-binding domain Computational biology Biology Biochemistry DNA binding site chemistry.chemical_compound Protein structure chemistry Structural Biology B3 domain DNA Binding domain
Zdroj:	Nature Structural Biology. 7:1139-1146
ISSN:	1072-8368
DOI:	10.1038/81999
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5255531f7fd7a225e821d1eb4f159770 https://doi.org/10.1038/81999 Zobrazit plný text záznamu Full text from SpringerLink