creators_name: Sarin, Jyoti
creators_name: Raghava, G.P.S.
creators_name: Chakraborti, Pradip K
type: article
datestamp: 2012-01-06 14:57:34
lastmod: 2012-01-06 15:18:07
metadata_visibility: show
title: Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin.
ispublished: pub
subjects: QR
full_text_status: restricted
keywords: ATP-binding cassette ATPase; polar amino acid; PstB; thermostability
note: Copyright of this article belongs to Wiley.
Supplemental material: See www.proteinscience.org.
abstract: The nucleotide-binding subunit of phosphate-specific transporter (PstB) from mesophilic bacterium, Mycobacterium tuberculosis, is a unique ATP-binding cassette (ABC) ATPase because of its unusual ability to hydrolyze ATP at high temperature. In an attempt to define the basis of thermostability, we took a theoretical approach and compared amino acid composition of this protein to that of other PstBs from available bacterial genomes. Interestingly, based on the content of polar amino acids, this protein clustered with the thermophiles.
date: 2003-09
date_type: published
publication: Protein science : a publication of the Protein Society
volume: 12
number: 9
publisher: Wiley
pagerange: 2118-20
refereed: TRUE
issn: 0961-8368
official_url: http://onlinelibrary.wiley.com/doi/10.1110/ps.0397603/pdf
related_url_url: http://onlinelibrary.wiley.com/doi/10.1110/ps.0397603/pdf
related_url_type: pub
citation:   Sarin, Jyoti and Raghava, G.P.S. and Chakraborti, Pradip K  (2003) Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin.  Protein science : a publication of the Protein Society, 12 (9).  pp. 2118-20.  ISSN 0961-8368     
document_url: http://crdd.osdd.net/open/236/1/chakraborti2003.pdf