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Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin.
 
Creator Sarin, Jyoti
Raghava, G.P.S.
Chakraborti, Pradip K
 
Subject QR Microbiology
 
Description 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.
 
Publisher Wiley
 
Date 2003-09
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/236/1/chakraborti2003.pdf
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
 
Relation http://onlinelibrary.wiley.com/doi/10.1110/ps.0397603/pdf
http://crdd.osdd.net/open/236/