Document Detail

Conformational Plasticity and Dynamics in the Generic Protein Folding Catalyst SlyD Unraveled by Single-Molecule FRET.
MedLine Citation:
PMID:  21596048     Owner:  NLM     Status:  Publisher    
The relation between conformational dynamics and chemistry in enzyme catalysis recently has received increasing attention. While, in the past, the mechanochemical coupling was mainly attributed to molecular motors, nowadays, it seems that this linkage is far more general. Single-molecule fluorescence methods are perfectly suited to directly evidence conformational flexibility and dynamics. By labeling the enzyme SlyD, a member of peptidyl-prolyl cis-trans isomerases of the FK506 binding protein type with an inserted chaperone domain, with donor and acceptor fluorophores for single-molecule fluorescence resonance energy transfer, we directly monitor conformational flexibility and conformational dynamics between the chaperone domain and the FK506 binding protein domain. We find a broad distribution of distances between the labels with two main maxima, which we attribute to an open conformation and to a closed conformation of the enzyme. Correlation analysis demonstrates that the conformations exchange on a rate in the 100-Hz range. With the aid from Monte Carlo simulations, we show that there must be conformational flexibility beyond the two main conformational states. Interestingly, neither the conformational distribution nor the dynamics is significantly altered upon binding of substrates or other known binding partners. Based on these experimental findings, we propose a model where the conformational dynamics is used to search the conformation enabling the chemical step, which also explains the remarkable substrate promiscuity connected with a high efficiency of this class of peptidyl-prolyl cis-trans isomerases.
Dana Kahra; Michael Kovermann; Christian Löw; Verena Hirschfeld; Caroline Haupt; Jochen Balbach; Christian Gerhard Hübner
Related Documents :
22052488 - A review of methods used for identifying structural changes in a large protein complex.
21498658 - Structural basis for the high-affinity inhibition of mammalian membranous adenylyl cycl...
21647838 - Hsp90 inhibitors and drugs from fragment and virtual screening.
9441608 - A comparison of the functional and interfacial properties of beta-casein and dephosphor...
22178918 - A fluorescent probe which allows highly specific thiol labeling at low ph.
19759058 - Proteome-wide substrate analysis indicates substrate exclusion as a mechanism to genera...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-5-7
Journal Detail:
Title:  Journal of molecular biology     Volume:  -     ISSN:  1089-8638     ISO Abbreviation:  -     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-5-20     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011. Published by Elsevier Ltd.
Institut für Physik, Universität zu Lübeck, Ratzeburger Allee 160, D-23564 Lübeck, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Testosterone and 11-ketotestosterone have different regulatory effects on electric communication sig...
Next Document:  Multiple POT1-TPP1 proteins coat and compact long telomeric single-stranded DNA.