A molecular switch in SecA protein couples ATP hydrolysis to protein translocation.

S, Karamanou; E, Vrontou; G, Sianidis; C, Baud; T, Roos; A, Kuhn; AS, Politou; A, Economou

doi:10.1046/j.1365-2958.1999.01686.x

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A molecular switch in SecA protein couples ATP hydrolysis to protein translocation.

Shared by NobleBlocks on Dec 1, 1999 • 12:00 AM UTC

Authors:

Karamanou S

Vrontou E

Sianidis G

Abstract

SecA, the dimeric ATPase subunit of bacterial protein translocase, catalyses translocation during ATP-driven membrane cycling at SecYEG. We now show that the SecA protomer comprises two structural modules: the ATPase N-domain, containing the nucleotide binding sites NBD1 and NBD2, and the regulatory...

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