4GX1
Crystal structure of the GsuK bound to ADP
Summary for 4GX1
Entry DOI | 10.2210/pdb4gx1/pdb |
Related | 4GVL 4GX0 4GX2 4GX5 |
Descriptor | TrkA domain protein, POTASSIUM ION, ZINC 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 | 250800.35 |
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 Cited by 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: 23240087DOI: 10.7554/eLife.00184 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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