6uwm | pdb_00006uwm

Single particle cryo-EM structure of KvAP

Loading... Status: waiting for Mol* initialization Structural highlights 6uwm is a 4 chain structure with sequence from Aerpx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: APE_0955 (AERPX) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KVAP_AERPE] Mediates a strong voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Publication Abstract from PubMed Conductance in voltage-gated ion channels is regulated by membrane voltage through structural domains known as voltage sensors. A single structural class of voltage sensor domain exists, but two different modes of voltage sensor attachment to the pore occur in nature: domain-swapped and non-domain-swapped. Since the more thoroughly studied Kv1-7, Nav and Cav channels have domain-swapped voltage sensors, much less is known about non-domain-swapped voltage-gated ion channels. In this paper, using cryo-EM, we show that KvAP from Aeropyrum pernix has non-domain-swapped voltage sensors as well as other unusual features. The new structure, together with previous functional data, suggests that KvAP and the Shaker channel, to which KvAP is most often compared, probably undergo rather different voltage-dependent conformational changes when they open. Cryo-EM structure of the KvAP channel reveals a non-domain-swapped voltage sensor topology.,Tao X, MacKinnon R Elife. 2019 Nov 22;8. pii: 52164. doi: 10.7554/eLife.52164. PMID:31755864 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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