1g29
From Proteopedia
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MALK
Overview
The members of the ABC transporter family transport a wide variety of, molecules into or out of cells and cellular compartments. Apart from a, translocation pore, each member possesses two similar nucleoside, triphosphate-binding subunits or domains in order to couple the, energy-providing reaction with transport. In the maltose transporter of, several Gram-negative bacteria and the archaeon Thermo coccus litoralis, the nucleoside triphosphate-binding subunit contains a C-terminal, regulatory domain. A dimer of the subunit is attached cytoplasmically to, the translocation pore. Here we report the crystal structure of this dimer, showing two bound pyrophosphate molecules at 1.9 A resolution. The dimer, forms by association of the ATPase domains, with the two regulatory, domains attached at opposite poles. Significant deviation from 2-fold, symmetry is seen at the interface of the dimer and in the regions, corresponding to those residues known to be in contact with the, translocation pore. The structure and its relationship to function are, discussed in the light of known mutations from the homologous Escherichia, coli and Salmonella typhimurium proteins.
About this Structure
1G29 is a Single protein structure of sequence from Thermococcus litoralis with NH4, MG, CL, NA, POP and DIO as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis., Diederichs K, Diez J, Greller G, Muller C, Breed J, Schnell C, Vonrhein C, Boos W, Welte W, EMBO J. 2000 Nov 15;19(22):5951-61. PMID:11080142
Page seeded by OCA on Sun Nov 25 00:42:51 2007
Categories: Single protein | Thermococcus litoralis | Boos, W. | Breed, J. | Diederichs, K. | Diez, J. | Greller, G. | Mueller, C. | Schnell, C. | Vonrhein, C. | Welte, W. | CL | DIO | MG | NA | NH4 | POP | Active transport | Atpase | Maltose uptake and regulation
