alexa Crystal structure of an N-terminal fragment of the DNA gyrase B protein.
Chemistry

Chemistry

Organic Chemistry: Current Research

Author(s): Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G

Abstract Share this page

Abstract The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, complexed with a nonhydrolysable ATP analogue, has been solved at 2.5 A 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 A hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction. This article was published in Nature and referenced in Organic Chemistry: Current Research

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

  • 3rd World Chemistry Conference
    September 11-12, 2017 Dallas, USA
  • 2nd International Conference on Biochemistry
    Sep 21-22, 2017 Macau, Hong Kong
  • Chemistry Congress 2017
    October 02-04, 2017 Vancouver, Canada

Relevant Topics

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords