Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Mol Biol. 2005 Sep 30;352(4):807-22.

Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase.

Author information

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge MA 02138, USA. maragakis@cmt.harvard.edu

Abstract

The plastic network model (PNM) is used to generate a conformational change pathway for Escherichia coli adenylate kinase based on two crystal structures, namely that of an open and a closed conformer. In this model, the energy basins corresponding to known conformers are connected at their lowest common energies. The results are used to evaluate and analyze the minimal energy pathways between these basins. The open to closed transition analysis provides an identification of hinges that is in agreement with the existing definitions based on the available X-ray structures. The elastic energy distribution and the C(alpha) pseudo-dihedral variation provide similar information on these hinges. The ensemble of the 45 published structures for this protein and closely related proteins is shown to always be within 3.0 A of the pathway, which corresponds to a conformational change between two end structures that differ by a C(alpha)-atom root-mean-squared deviation of 7.1A.

PMID:
16139299
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk