4L74

Ca2+-bound MthK RCK domain at 1.9 Angstrom with single ligand

Summary for 4L74

• Entry DOI: 10.2210/pdb4l74/pdb
• Related: 4L73 4L75 4L76
• Descriptor: Calcium-gated potassium channel MthK, CALCIUM ION (3 entities in total)
• Functional Keywords: rossmann fold, regulatory domain, calcium binding, membrane-associated, metal transport
• Biological source: Methanothermobacter thermautotrophicus
• Cellular location: Cell membrane; Multi-pass membrane protein: O27564
• Total number of polymer chains: 2
• Total formula weight: 53855.34

Authors

Smith, F.J.,Cingolani, G.,Rothberg, B.S. (deposition date: 2013-06-13, release date: 2013-10-23, Last modification date: 2023-09-20)

Primary citation

Smith, F.J.,Pau, V.P.,Cingolani, G.,Rothberg, B.S.
Structural basis of allosteric interactions among Ca(2+)-binding sites in a K(+) channel RCK domain.
Nat Commun, 4:2621-2621, 2013

PubMed Abstract: Ligand binding sites within proteins can interact by allosteric mechanisms to modulate binding affinities and control protein function. Here we present crystal structures of the regulator of K+ conductance (RCK) domain from a K+ channel, MthK, which reveal the structural basis of allosteric coupling between two Ca2+ regulatory sites within the domain. Comparison of RCK domain crystal structures in a range of conformations and with different numbers of regulatory Ca2+ ions bound, combined with complementary electrophysiological analysis of channel gating, suggests chemical interactions that are important for modulation of ligand binding and subsequent channel opening.

PubMed: 24126388
DOI: 10.1038/ncomms3621

Experimental method

X-RAY DIFFRACTION (1.841 Å)