› 6zhh

X-ray diffraction
3Å resolution

Ca2+-ATPase from Listeria Monocytogenes with G4 insertion.

Released:
DOI: 10.2210/pdb6zhh/pdb
Model geometry
Fit model/data
PDB entry 6zhh coloured by chain, front view.
PDB entry 6zhh coloured by chain, side view.
PDB entry 6zhh coloured by chain, top view.
Source organism: Listeria monocytogenes
Primary publication:
The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation.
Hansen SB, Dyla M, Neumann C, Quistgaard EMH, Andersen JL, Kjaergaard M, Nissen P
J Mol Biol 433 167015 (2021)
PMID: 33933469

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate + Ca(2+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calcium-transporting ATPase lmo0841 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 911 amino acids
Theoretical weight: 99.34 KDa
Source organism: Listeria monocytogenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8Y8Q5 (Residues: 2-44, 45-880; Coverage: 100%)
Gene name: lmo0841
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand BEF 8 x BEF
Ligand MG 8 x MG
Ligand PCW 15 x PCW
Ligand CE1 7 x CE1
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P21
Unit cell:
a: 74.062Å b: 188.499Å c: 350.007Å
α: 90° β: 91.94° γ: 90°
R-values:
R R work R free
0.255 0.255 0.285
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.
Brown et al. (2021)
3 other articles

1 mention without citation

Uncovering the antimalarial potential of toad venoms through a bioassay-guided fractionation process.
Wells et al. (2022)