alexa Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution.


Journal of Physical Chemistry & Biophysics

Author(s): Wang J, Boisvert DC

Abstract Share this page

Abstract Nucleotide regulates the affinity of the bacterial chaperonin GroEL for protein substrates. GroEL binds protein substrates with high affinity in the absence of ATP and with low affinity in its presence. We report the crystal structure of (GroEL-KMgATP)(14) refined to 2.0 A resolution in which the ATP triphosphate moiety is directly coordinated by both K(+) and Mg(2+). Upon the binding of KMgATP, we observe previously unnoticed domain rotations and a 102 degrees rotation of the apical domain surface helix I. Two major consequences are a large lateral displacement of, and a dramatic reduction of hydrophobicity in, the apical domain surface. These results provide a basis for the nucleotide-dependent regulation of protein substrate binding and suggest a mechanism for GroEL-assisted protein folding by forced unfolding. Copyright 2003 Elsevier Science Ltd.
This article was published in J Mol Biol and referenced in Journal of Physical Chemistry & Biophysics

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

  • 5th International Conference and Exhibition on Physical Medicine & Rehabilitation
    Aug 14-16, 2017 Los Angeles, USA
  • 2nd International Conference on Physics
    Aug 28-30, 2017 Brussels, Belgium
  • 5th Global Chemistry Congress
    September 04-06, 2017 London, UK
  • 3rd World Chemistry Conference
    September 11-12, 2017 Dallas, USA
  • Global Conference on Physical Chemistry
    September 18-19, 2017 Dublin, Ireland
  • 2nd International Conference on Applied Chemistry  
    October 16-17, 2017 Toronto, Canada
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