3ldc

From Proteopedia
Revision as of 11:35, 6 September 2023 by OCA (talk | contribs)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search

High resolution open MthK pore structure crystallized in 100 mM K+High resolution open MthK pore structure crystallized in 100 mM K+

Structural highlights

3ldc is a 1 chain structure with sequence from Methanothermobacter thermautotrophicus str. Delta H. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.45Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MTHK_METTH Calcium-gated potassium channel.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

K+ channels are highly selective for K+ over Na+. Here we present several crystal structures of the MthK K+ channel pore at up to 1.45-A resolution. The MthK selectivity filter maintains a conductive conformation even in the absence of K+, allowing the channel to conduct Na+. The high-resolution structures, along with single-channel recordings, allow for an accurate analysis of how K+ competes with Na+ in a conductive selectivity filter. At high K+ concentrations, two K+ ions equivalently occupy the four sites in the selectivity filter, whereas at low K+/high Na+ concentrations, a single K+ ion remains bound in the selectivity filter, preferably at site 1 or site 3. This single K+ binding at low concentration effectively blocks the permeation of Na+, providing a structural basis for the anomalous mole-fraction effect, a key property of multi-ion pores.

Novel insights into K+ selectivity from high-resolution structures of an open K+ channel pore.,Ye S, Li Y, Jiang Y Nat Struct Mol Biol. 2010 Aug;17(8):1019-23. Epub 2010 Aug 1. PMID:20676101[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Ye S, Li Y, Jiang Y. Novel insights into K+ selectivity from high-resolution structures of an open K+ channel pore. Nat Struct Mol Biol. 2010 Aug;17(8):1019-23. Epub 2010 Aug 1. PMID:20676101 doi:10.1038/nsmb.1865

3ldc, resolution 1.45Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA