4MLB
Reverse polarity of binding pocket suggests different function of a MOP superfamily transporter from Pyrococcus furiosus Vc1 (DSM3638)
Summary for 4MLB
| Entry DOI | 10.2210/pdb4mlb/pdb |
| Descriptor | PF0708, PENTAETHYLENE GLYCOL MONODECYL ETHER, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | lipid translocase, flippase, membrane protein, transport protein |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 4 |
| Total formula weight | 231846.29 |
| Authors | Malviya, V.N.,Nonaka, T.,Muenke, C.,Koepke, J.,Michel, H. (deposition date: 2013-09-06, release date: 2013-09-25, Last modification date: 2023-09-20) |
| Primary citation | Zakrzewska, S.,Mehdipour, A.R.,Malviya, V.N.,Nonaka, T.,Koepke, J.,Muenke, C.,Hausner, W.,Hummer, G.,Safarian, S.,Michel, H. Inward-facing conformation of a multidrug resistance MATE family transporter. Proc.Natl.Acad.Sci.USA, 116:12275-12284, 2019 Cited by PubMed Abstract: 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 (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. PubMed: 31160466DOI: 10.1073/pnas.1904210116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.349 Å) |
Structure validation
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