6D0K
Crystal structure of a CLC-type fluoride/proton antiporter, E118Q mutant
Summary for 6D0K
| Entry DOI | 10.2210/pdb6d0k/pdb |
| Descriptor | CLC-type fluoride/proton antiporter, Monobody, DECYL-BETA-D-MALTOPYRANOSIDE, ... (6 entities in total) |
| Functional Keywords | fluoride/proton antiporter, clc membrane protein, transport protein |
| Biological source | Enterococcus casseliflavus (strain EC10) More |
| Total number of polymer chains | 4 |
| Total formula weight | 114222.67 |
| Authors | Last, N.B.,Stockbridge, R.B.,Wilson, A.E.,Shane, T.,Kolmakova-Partensky, L.,Koide, A.,Koide, S.,Miller, C. (deposition date: 2018-04-10, release date: 2018-07-04, Last modification date: 2023-10-04) |
| Primary citation | Last, N.B.,Stockbridge, R.B.,Wilson, A.E.,Shane, T.,Kolmakova-Partensky, L.,Koide, A.,Koide, S.,Miller, C. A CLC-type F-/H+antiporter in ion-swapped conformations. Nat. Struct. Mol. Biol., 25:601-606, 2018 Cited by PubMed Abstract: Fluoride/proton antiporters of the CLC family combat F toxicity in bacteria by exporting this halide from the cytoplasm. These transporters belong to the widespread CLC superfamily but display transport properties different from those of the well-studied Cl/H antiporters. Here, we report a structural and functional investigation of these F-transport proteins. Crystal structures of a CLC homolog from Enterococcus casseliflavus are captured in two conformations with simultaneous accessibility of F and H ions via separate pathways on opposite sides of the membrane. Manipulation of a key glutamate residue critical for H and F transport reverses the anion selectivity of transport; replacement of the glutamate with glutamine or alanine completely inhibits F and H transport while allowing for rapid uncoupled flux of Cl. The structural and functional results lead to a 'windmill' model of CLC antiport wherein F and H simultaneously move through separate ion-specific pathways that switch sidedness during the transport cycle. PubMed: 29941917DOI: 10.1038/s41594-018-0082-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.35 Å) |
Structure validation
Download full validation report
