4mlb

Reverse polarity of binding pocket suggests different function of a MOP superfamily transporter from Pyrococcus furiosus Vc1 (DSM3638)

spinqualitylabelsall models 4mlb, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mlb is a 4 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.349Å Ligands: CL, CXE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8U2X0_PYRFU Publication Abstract from PubMed Multidrug and toxic compound extrusion (MATE) transporters mediate excretion of xenobiotics and toxic metabolites, thereby conferring multidrug resistance in bacterial pathogens and cancer cells. Structural information on the alternate conformational states and knowledge of the detailed mechanism of MATE transport are of great importance for drug development. However, the structures of MATE transporters are only known in V-shaped outward-facing conformations. Here, we present the crystal structure of a MATE transporter from Pyrococcus furiosus (PfMATE) in the long-sought-after inward-facing state, which was obtained after crystallization in the presence of native lipids. Transition from the outward-facing state to the inward-facing state involves rigid body movements of transmembrane helices (TMs) 2-6 and 8-12 to form an inverted V, facilitated by a loose binding of TM1 and TM7 to their respective bundles and their conformational flexibility. The inward-facing structure of PfMATE in combination with the outward-facing one supports an alternating access mechanism for the MATE family transporters. Inward-facing conformation of a multidrug resistance MATE family transporter.,Zakrzewska S, Mehdipour AR, Malviya VN, Nonaka T, Koepke J, Muenke C, Hausner W, Hummer G, Safarian S, Michel H Proc Natl Acad Sci U S A. 2019 Jun 3. pii: 1904210116. doi:, 10.1073/pnas.1904210116. PMID:31160466 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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