Crystal structure of an N-terminal fragment of the DNA gyrase B protein View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-06

AUTHORS

Dale B. Wigley, Gideon J. Davies, Eleanor J. Dodson, Anthony Maxwell, Guy Dodson

ABSTRACT

The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, com-plexed with a nonhn/drolysable ATP analogue, has been solved at 2.5 Å resolution. It consists of two domains, both containing novel protein folds. The protein fragment forms a dimer, whose N-terminal domains are responsible for ATP binding and hydrolysis. The C-terminal domains form the sides of a 20 Å hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction. More... »

PAGES

624-629

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/351624a0

DOI

http://dx.doi.org/10.1038/351624a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010938729

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1646964


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