creators_name: Taneja, Bhupesh
creators_name: Mande, S C
type: article
datestamp: 2012-01-04 14:55:49
lastmod: 2015-01-09 11:13:07
metadata_visibility: show
title: Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10.
ispublished: pub
subjects: QR
full_text_status: restricted
keywords: chaperonin-10dome loopmetastable stateMycobacterium tuberculosis structural plasticity
note: Copyright of this article belongs to OUP.
abstract: Chaperonin-10s possess a highly flexible segment of approximately 10 residues that covers their dome-like structure and closes the central cavity of the chaperonin assembly. The dome loop is believed to contribute to the plasticity of their oligomeric structure. We have exploited the presence of a single tryptophan residue occurring in the dome loop of Mycobacterium tuberculosis chaperonin-10 (cpn-10), and through intrinsic fluorescence measurements show that in the absence of metal ions, the tryptophan is almost fully solvent exposed at neutral pH. The dome loop, however, assumes a closed conformation in the presence of metal ions, or at low pH. These changes are fully reversed in the presence of chelating agents such as EDTA, confirming the role of cations in modulating the metastable states of cpn-10.
date: 2001-06
date_type: published
publication: Protein engineering
volume: 14
number: 6
publisher: Oxford University Press
pagerange: 391-5
refereed: TRUE
issn: 0269-2139
official_url: http://peds.oxfordjournals.org/content/14/6/391.long
related_url_url: http://peds.oxfordjournals.org/content/14/6/391.long
related_url_type: pub
citation:   Taneja, Bhupesh and Mande, S C  (2001) Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10.  Protein engineering, 14 (6).  pp. 391-5.  ISSN 0269-2139     
document_url: http://crdd.osdd.net/open/293/1/mande2001.1.pdf