Direct demonstration that ATP is in contact with Cys-137 in chaperonin GroEL.
The nonhydrolyzable ATP analogue ATP gamma S (adenosine 5'-3-O-(thio)triphosphate) is affinity cross-linked to GroEL by formation of a disulfide bridge in a peroxide-promoted reaction. By replacing with serine each of 3 cysteine residues in GroEL, it is shown that ATP gamma S specifically cross-links to Cys-137. It is thus demonstrated that the ATP bound to GroEL is in direct contact with Cys-137.
Bochkareva
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Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Horovitz
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Girshovich
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D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001483:Base Sequence; D018834:Chaperonin 60; D003432:Cross-Linking Reagents; D003545:Cysteine / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides
D001426:Bacterial Proteins; D018834:Chaperonin 60; D003432:Cross-Linking Reagents; D006360:Heat-Shock Proteins; D009838:Oligodeoxyribonucleotides; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate; D003545:Cysteine