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FOR THE RECORD

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

Institute of Microbial Technology, Chandigarh 160 036, India

Reprint requests to: Pradip K. Chakraborti, Institute of Microbial Technology, Sector 39A, Chandigarh 160 036, India; e-mail: pradip{at}imtech.res.in; fax: 91-172-690585.

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.

Keywords: ATP-binding cassette ATPase; polar amino acid; PstB; thermostability

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