PDBsum entry 4l76

Metal transport

PDB id: 4l76

Contents

Protein chains

(+ 0 more) 227 a.a.

Metals

_CA ×13

_NA ×2

Waters ×1

PDB id:

4l76

Name:

Metal transport

Title:

Ca2+-bound e212q mutant mthk rck domain

Structure:

Calcium-gated potassium channel mthk. Chain: a, b, c, d, e, f. Fragment: rck domain (unp residues 107-336). Engineered: yes. Mutation: yes

Source:

Methanothermobacter thermautotrophicus. Organism_taxid: 187420. Strain: atcc 29096 / dsm 1053 / jcm 10044 / nbrc 100330 / delta h. Gene: mthk, mth_1520. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.99Å R-factor: 0.220 R-free: 0.263

Authors:

F.J.Smith,B.S.Rothberg

Key ref:

F.J.Smith et al. (2013). Structural basis of allosteric interactions among Ca2+-binding sites in a K+ channel RCK domain. Nat Commun, 4, 2621. PubMed id: 24126388 DOI: 10.1038/ncomms3621

Date:

13-Jun-13 Release date: 23-Oct-13

Protein chains

O27564  (MTHK_METTH) -  Calcium-gated potassium channel MthK from Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

Seq: 336 a.a.

Struc: 227 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/ncomms3621

Nat Commun 4:2621 (2013)

PubMed id: 24126388

Structural basis of allosteric interactions among Ca2+-binding sites in a K+ channel RCK domain.

F.J.Smith, V.P.Pau, G.Cingolani, B.S.Rothberg.

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 Ca(2+) regulatory sites within the domain. Comparison of RCK domain crystal structures in a range of conformations and with different numbers of regulatory Ca(2+) 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.