6A6N
Crystal structure of an inward-open apo state of the eukaryotic ABC multidrug transporter CmABCB1
Summary for 6A6N
| Entry DOI | 10.2210/pdb6a6n/pdb |
| Descriptor | ATP-binding cassette, sub-family B, member 1, DECYL-BETA-D-MALTOPYRANOSIDE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
| Functional Keywords | alpha-helical, transport protein |
| Biological source | Cyanidioschyzon merolae strain 10D (Red alga) |
| Total number of polymer chains | 1 |
| Total formula weight | 68099.00 |
| Authors | Kato, H.,Nakatsu, T.,Kodan, A. (deposition date: 2018-06-28, release date: 2019-01-16, Last modification date: 2023-11-22) |
| Primary citation | Kodan, A.,Yamaguchi, T.,Nakatsu, T.,Matsuoka, K.,Kimura, Y.,Ueda, K.,Kato, H. Inward- and outward-facing X-ray crystal structures of homodimeric P-glycoprotein CmABCB1. Nat Commun, 10:88-88, 2019 Cited by PubMed Abstract: P-glycoprotein extrudes a large variety of xenobiotics from the cell, thereby protecting tissues from their toxic effects. The machinery underlying unidirectional multidrug pumping remains unknown, largely due to the lack of high-resolution structural information regarding the alternate conformational states of the molecule. Here we report a pair of structures of homodimeric P-glycoprotein: an outward-facing conformational state with bound nucleotide and an inward-facing apo state, at resolutions of 1.9 Å and 3.0 Å, respectively. Features that can be clearly visualized at this high resolution include ATP binding with octahedral coordination of Mg; an inner chamber that significantly changes in volume with the aid of tight connections among transmembrane helices (TM) 1, 3, and 6; a glutamate-arginine interaction that stabilizes the outward-facing conformation; and extensive interactions between TM1 and TM3, a property that distinguishes multidrug transporters from floppases. These structural elements are proposed to participate in the mechanism of the transporter. PubMed: 30622258DOI: 10.1038/s41467-018-08007-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.02 Å) |
Structure validation
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