The University of Southampton
University of Southampton Institutional Repository

Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer

Pilak, Oliver, Harrop, Stephen J., Siddiqui, Khawar S., Chong, Kevin, De Francisci, Davide, Burg, Dominic, Williams, Timothy J, Cavicchioli, Ricardo and Curmi, Paul M G (2011) Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer Environmental Microbiology, 13, (8), pp. 2232-49. (doi:10.1111/j.1462-2920.2011.02477.x). (PMID:21477108).

Record type: Article

Abstract

Archaea are abundant in permanently cold environments. The Antarctic methanogen, Methanococcoides burtonii, has proven an excellent model for studying molecular mechanisms of cold adaptation. Methanococcoides burtonii contains three group II chaperonins that diverged prior to its closest orthologues from mesophilic Methanosarcina spp. The relative abundance of the three chaperonins shows little dependence on organism growth temperature, except at the highest temperatures, where the most thermally stable chaperonin increases in abundance. In vitro and in vivo, the M. burtonii chaperonins are predominantly monomeric, with only 23-33% oligomeric, thereby differing from other archaea where an oligomeric ring form is dominant. The crystal structure of an N-terminally truncated chaperonin reveals a monomeric protein with a fully open nucleotide binding site. When compared with closed state group II chaperonin structures, a large-scale ? 30° rotation between the equatorial and intermediate domains is observed resulting in an open nucleotide binding site. This is analogous to the transition observed between open and closed states of group I chaperonins but contrasts with recent archaeal group II chaperonin open state ring structures. The predominance of monomeric form and the ability to adopt a fully open nucleotide site appear to be unique features of the M. burtonii group II chaperonins.

Full text not available from this repository.

More information

Published date: August 2011
Organisations: Molecular and Cellular

Identifiers

Local EPrints ID: 338905
URI: http://eprints.soton.ac.uk/id/eprint/338905
ISSN: 1462-2920
PURE UUID: 2782f6b0-86eb-4534-a92f-660cdd4efbb4

Catalogue record

Date deposited: 17 May 2012 15:30
Last modified: 18 Jul 2017 05:56

Export record

Altmetrics

Contributors

Author: Oliver Pilak
Author: Stephen J. Harrop
Author: Khawar S. Siddiqui
Author: Kevin Chong
Author: Davide De Francisci
Author: Dominic Burg
Author: Timothy J Williams
Author: Ricardo Cavicchioli
Author: Paul M G Curmi

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×