6C3O
Cryo-EM structure of human KATP bound to ATP and ADP in quatrefoil form
Summary for 6C3O
| Entry DOI | 10.2210/pdb6c3o/pdb |
| EMDB information | 7338 |
| Descriptor | ATP-sensitive inward rectifier potassium channel 11, ATP-binding cassette sub-family C member 8, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | atp-dependent potassium channel kir6.2 sur1 atp adp, transport protein |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Membrane; Multi-pass membrane protein: Q14654 Cell membrane ; Multi-pass membrane protein : Q09428 |
| Total number of polymer chains | 8 |
| Total formula weight | 895376.33 |
| Authors | |
| Primary citation | Lee, K.P.K.,Chen, J.,MacKinnon, R. Molecular structure of human KATP in complex with ATP and ADP Elife, 6:-, 2017 Cited by PubMed Abstract: In many excitable cells, KATP channels respond to intracellular adenosine nucleotides: ATP inhibits while ADP activates. We present two structures of the human pancreatic KATP channel, containing the ABC transporter SUR1 and the inward-rectifier K channel Kir6.2, in the presence of Mg and nucleotides. These structures, referred to as quatrefoil and propeller forms, were determined by single-particle cryo-EM at 3.9 Å and 5.6 Å, respectively. In both forms, ATP occupies the inhibitory site in Kir6.2. The nucleotide-binding domains of SUR1 are dimerized with Mg-ATP in the degenerate site and Mg-ADP in the consensus site. A lasso extension forms an interface between SUR1 and Kir6.2 adjacent to the ATP site in the propeller form and is disrupted in the quatrefoil form. These structures support the role of SUR1 as an ADP sensor and highlight the lasso extension as a key regulatory element in ADP's ability to override ATP inhibition. PubMed: 29286281DOI: 10.7554/eLife.32481 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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