› 3mfy

X-ray diffraction
2.35Å resolution

Structural characterization of the subunit A mutant F236A of the A-ATP synthase from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb3mfy/pdb
PDB entry 3mfy coloured by chain, front view.
PDB entry 3mfy coloured by chain, side view.
PDB entry 3mfy coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide binding.
Kumar A, Manimekalai MS, Balakrishna AM, Priya R, Biuković G, Jeyakanthan J, Grüber G
J Mol Biol 401 892-905 (2010)
PMID: 20615420

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129601 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

3 bound ligands:
Ligand MPD 5 x MPD
Ligand TRS 1 x TRS
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P43212
Unit cell:
a: 127.535Å b: 127.535Å c: 106.785Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.222 0.279
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.
Manimekalai et al. (2011)
1 more