4GX0

Crystal structure of the GsuK L97D mutant

Summary for 4GX0

• Entry DOI: 10.2210/pdb4gx0/pdb
• Related: 4GVL 4GX1 4GX2 4GX5
• Related PRD ID: PRD_900001
• Descriptor: TrkA domain protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, POTASSIUM ION, ... (8 entities in total)
• Functional Keywords: membrane protein, ion channel, adp binding, nad binding, membrane, transport protein
• Biological source: Geobacter sulfurreducens
• Total number of polymer chains: 4
• Total formula weight: 249577.70

Authors

Kong, C.,Zeng, W.,Ye, S.,Chen, L.,Sauer, D.B.,Lam, Y.,Derebe, M.G.,Jiang, Y. (deposition date: 2012-09-03, release date: 2012-12-26, Last modification date: 2024-02-28)

Primary citation

Kong, C.,Zeng, W.,Ye, S.,Chen, L.,Sauer, D.B.,Lam, Y.,Derebe, M.G.,Jiang, Y.
Distinct gating mechanisms revealed by the structures of a multi-ligand gated K(+) channel.
elife, 1:e00184-e00184, 2012

PubMed Abstract: The gating ring-forming RCK domain regulates channel gating in response to various cellular chemical stimuli in eukaryotic Slo channel families and the majority of ligand-gated prokaryotic K(+) channels and transporters. Here we present structural and functional studies of a dual RCK-containing, multi-ligand gated K(+) channel from Geobacter sulfurreducens, named GsuK. We demonstrate that ADP and NAD(+) activate the GsuK channel, whereas Ca(2+) serves as an allosteric inhibitor. Multiple crystal structures elucidate the structural basis of multi-ligand gating in GsuK, and also reveal a unique ion conduction pore with segmented inner helices. Structural comparison leads us to propose a novel pore opening mechanics that is distinct from other K(+) channels.DOI:http://dx.doi.org/10.7554/eLife.00184.001.

PubMed: 23240087
DOI: 10.7554/eLife.00184

Experimental method

X-RAY DIFFRACTION (2.601 Å)