1L2T

Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette

1L2T の概要

• エントリーDOI: 10.2210/pdb1l2t/pdb
• 分子名称: Hypothetical ABC transporter ATP-binding protein MJ0796, SODIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: abc transporters, atpase, walker-a, nbd, transport protein
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54385.92

構造登録者

Smith, P.C.,Karpowich, N.,Rosen, J.,Hunt, J.F. (登録日: 2002-02-24, 公開日: 2002-07-24, 最終更新日: 2024-02-14)

主引用文献

Smith, P.C.,Karpowich, N.,Millen, L.,Moody, J.E.,Rosen, J.,Thomas, P.J.,Hunt, J.F.
ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer.
Mol.Cell, 10:139-149, 2002

PubMed Abstract: 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 dimer formed by the E171Q 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.

PubMed: 12150914
DOI: 10.1016/S1097-2765(02)00576-2

実験手法

X-RAY DIFFRACTION (1.9 Å)