The EMBO Journal Vol. 19 No. 22 pp. 5951±5961, 2000 Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis Kay Diederichs, Joachim Diez, ®brosis transmembrane conductance regulator (CFTR) Gerhard Greller, Christian MuÈ ller1, involved in the inherited disease cystic ®brosis, sterol Jason Breed2, Christoph Schnell, transporters, eye pigment precursor importers and protein Clemens Vonrhein3, Winfried Boos and exporters. Even though the arrayof substrates seems Wolfram Welte4 endless and the molecular architecture can be rather diverse, the ATPase module is an essential and conserved Fachbereich Biologie, UniversitaÈt Konstanz, M656, D-78457 Konstanz, subunit of all transporters. Its sequence features are the 1 Germany, School of Bioscience, Cardiff University, 10 Museums main basis for the identi®cation of new familymembers Avenue, PO Box 911, Cardiff CF10 3US, 2Astra Zeneca, Mereside, Maccles®eld SK10 4TG and 3Global Phasing Ltd, Sheraton House, (Holland and Blight, 1999). Castle Park, Cambridge CB3 0AX, UK A subfamilyof ABC transporters are binding protein- dependent systems that are ubiquitous in eubacteria and 4Corresponding author e-mail:
[email protected] archaea, where theycatalysethe high-af®nityuptake of small polar substrates into the cell. One of the best studied The members of the ABC transporter family trans- examples is the E.coli maltose±maltodextrin system (Boos port a wide variety of molecules into or out of cells and Lucht, 1996; Boos and Shuman, 1998). It consists of a and cellular compartments. Apart from a trans- binding protein (MalE) as its major substrate recognition location pore, each member possesses two similar site, located in the periplasm.