› 5hxr

X-ray diffraction
2.46Å resolution

Structural mechanisms of extracellular ion exchange and induced binding-site occlusion in the sodium-calcium exchanger NCX_Mj soaked with 2.5 mM Na+ and 10mM Ca2+

Released:
DOI: 10.2210/pdb5hxr/pdb
PDB entry 5hxr coloured by chain, front view.
PDB entry 5hxr coloured by chain, side view.
PDB entry 5hxr coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii DSM 2661
Primary publication:
Mechanism of extracellular ion exchange and binding-site occlusion in a sodium/calcium exchanger.
Liao J, Marinelli F, Lee C, Huang Y, Faraldo-Gómez JD, Jiang Y
Nat Struct Mol Biol 23 590-599 (2016)
PMID: 27183196

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176431 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized membrane protein MJ0091 Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 32.03 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57556 (Residues: 1-300; Coverage: 99%)
Gene name: MJ0091
Sequence domains: Sodium/calcium exchanger protein
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CA 2 x CA
Ligand OLC 2 x OLC
Ligand MYS 9 x MYS
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 49.7Å b: 72.522Å c: 96.942Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.26
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Hydrogen-Deuterium Exchange Mass-Spectrometry of Secondary Active Transporters: From Structural Dynamics to Molecular Mechanisms.
Giladi et al. (2020)
6 more

5 mentions without citation

Structure-Functional Basis of Ion Transport in Sodium-Calcium Exchanger (NCX) Proteins.
Giladi et al. (2016)
4 more