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Title: Synchrotron Protein Footprinting Supports Substrate Translocation by ClpA via ATP-Induced Movements of the D2 Loop

Abstract

Synchrotron X-ray protein footprinting is used to study structural changes upon formation of the ClpA hexamer. Comparative solvent accessibilities between ClpA monomer and ClpA hexamer samples are in agreement throughout most of the sequence, with calculations based on two previously proposed hexameric models. The data differ substantially from the proposed models in two parts of the structure: the D1 sensor 1 domain and the D2 loop region. The results suggest that these two regions can access alternate conformations in which their solvent protection is greater than that in the structural models based on crystallographic data. In combination with previously reported structural data, the footprinting data provide support for a revised model in which the D2 loop contacts the D1 sensor 1 domain in the ATP-bound form of the complex. These data provide the first direct experimental support for the nucleotide-dependent D2 loop conformational change previously proposed to mediate substrate translocation.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959987
Report Number(s):
BNL-82973-2009-JA
TRN: US1005859
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
Structure
Additional Journal Information:
Journal Volume: 16
Country of Publication:
United States
Language:
English
Subject:
43 PARTICLE ACCELERATORS; CONFORMATIONAL CHANGES; MONOMERS; PROTEINS; SOLVENTS; STRUCTURAL MODELS; SUBSTRATES; SYNCHROTRONS; TRANSLOCATION; national synchrotron light source

Citation Formats

Bohon,J., Jennings, L., Phillips, C., Licht, S., and Chance, M. Synchrotron Protein Footprinting Supports Substrate Translocation by ClpA via ATP-Induced Movements of the D2 Loop. United States: N. p., 2008. Web. doi:10.1016/j.str.2008.04.016.
Bohon,J., Jennings, L., Phillips, C., Licht, S., & Chance, M. Synchrotron Protein Footprinting Supports Substrate Translocation by ClpA via ATP-Induced Movements of the D2 Loop. United States. doi:10.1016/j.str.2008.04.016.
Bohon,J., Jennings, L., Phillips, C., Licht, S., and Chance, M. Tue . "Synchrotron Protein Footprinting Supports Substrate Translocation by ClpA via ATP-Induced Movements of the D2 Loop". United States. doi:10.1016/j.str.2008.04.016.
@article{osti_959987,
title = {Synchrotron Protein Footprinting Supports Substrate Translocation by ClpA via ATP-Induced Movements of the D2 Loop},
author = {Bohon,J. and Jennings, L. and Phillips, C. and Licht, S. and Chance, M.},
abstractNote = {Synchrotron X-ray protein footprinting is used to study structural changes upon formation of the ClpA hexamer. Comparative solvent accessibilities between ClpA monomer and ClpA hexamer samples are in agreement throughout most of the sequence, with calculations based on two previously proposed hexameric models. The data differ substantially from the proposed models in two parts of the structure: the D1 sensor 1 domain and the D2 loop region. The results suggest that these two regions can access alternate conformations in which their solvent protection is greater than that in the structural models based on crystallographic data. In combination with previously reported structural data, the footprinting data provide support for a revised model in which the D2 loop contacts the D1 sensor 1 domain in the ATP-bound form of the complex. These data provide the first direct experimental support for the nucleotide-dependent D2 loop conformational change previously proposed to mediate substrate translocation.},
doi = {10.1016/j.str.2008.04.016},
journal = {Structure},
number = ,
volume = 16,
place = {United States},
year = {2008},
month = {1}
}