5VK6

Open conformation of KcsA non-inactivating E71A mutant

Summary for 5VK6

• Entry DOI: 10.2210/pdb5vk6/pdb
• Related: 5VKE 5VKH
• Descriptor: Antibody Heavy Chain, Antibody Light Chain, pH-gated potassium channel KcsA, ... (7 entities in total)
• Functional Keywords: kcsa, open, non-inactivating, potassium channel, immune system-transport protein complex, immune system/transport protein
• Biological source: Streptomyces lividans; More
• Total number of polymer chains: 3
• Total formula weight: 57813.42

Authors

Cuello, L.G.,Perozo, E. (deposition date: 2017-04-21, release date: 2017-12-06, Last modification date: 2024-10-23)

Primary citation

Cuello, L.G.,Cortes, D.M.,Perozo, E.
The gating cycle of a K+ channel at atomic resolution.
Elife, 6:-, 2017

PubMed Abstract: C-type inactivation in potassium channels helps fine-tune long-term channel activity through conformational changes at the selectivity filter. Here, through the use of cross-linked constitutively open constructs, we determined the structures of KcsA's mutants that stabilize the selectivity filter in its conductive (E71A, at 2.25 Å) and deep C-type inactivated (Y82A at 2.4 Å) conformations. These structural snapshots represent KcsA's transient open-conductive (O/O) and the stable open deep C-type inactivated states (O/I), respectively. The present structures provide an unprecedented view of the selectivity filter backbone in its collapsed deep C-type inactivated conformation, highlighting the close interactions with structural waters and the local allosteric interactions that couple activation and inactivation gating. Together with the structures associated with the closed-inactivated state (C/I) and in the well-known closed conductive state (C/O), this work recapitulates, at atomic resolution, the key conformational changes of a potassium channel pore domain as it progresses along its gating cycle.

PubMed: 29165243
DOI: 10.7554/eLife.28032

Experimental method

X-RAY DIFFRACTION (2.25 Å)