Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin.
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.
Sarin
Jyoti
J
Institute of Microbial Technology, Chandigarh 160 036, India.
Raghava
Gajendra P S
GP
Chakraborti
Pradip K
PK
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry*; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry; D000596:Amino Acids / Q000737:chemistry*; D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry*; D019992:Databases as Topic; D016680:Genome, Bacterial; D006868:Hydrolysis; D009169:Mycobacterium tuberculosis / Q000378:metabolism; D010802:Phylogeny; D011487:Protein Conformation; D013045:Species Specificity; D013696:Temperature
D018528:ATP-Binding Cassette Transporters; D000596:Amino Acids; D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C120060:phosphate import ATP-binding protein, Bacteria