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Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC–ATPase of mesophilic origin
Author(s) -
Sarin Jyoti,
Raghava Gajendra P.S.,
Chakraborti Pradip K.
Publication year - 2003
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.0397603
Subject(s) - thermostability , thermophile , atpase , biochemistry , amino acid , atp binding cassette transporter , mesophile , nucleotide , chemistry , protein subunit , biology , enzyme , bacteria , transporter , genetics , gene
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.