Journal
MOLECULAR CELL
Volume 10, Issue 1, Pages 139-149Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(02)00576-2
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Funding
- NIDDK NIH HHS [R01 DK049835] Funding Source: Medline
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It has been proposed that the reaction cycle of ATP binding cassette (ABC) transporters is driven by dimerization of their ABC motor domains upon binding ATP at their mutual interface. However, no such ATP sandwich complex has been observed for an ABC from an ABC transporter. In this paper, we report the crystal structure of a stable climer formed by the El 71 Q mutant of the MJ0796 ABC, which is hydrolytically inactive due to mutation of the catalytic base. The structure shows a symmetrical dimer in which two ATP molecules are each sandwiched between the Walker A motif in one subunit and the LSGGQ signature motif in the other subunit. These results establish the stereochemical basis of the power stroke of ABC transporter pumps.
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