› 3se0

X-ray diffraction
2.62Å resolution

Structural characterization of the subunit A mutant F508W of the A-ATP synthase from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb3se0/pdb
PDB entry 3se0 coloured by chain, front view.
PDB entry 3se0 coloured by chain, side view.
PDB entry 3se0 coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy.
Tadwal VS, Manimekalai MS, Grüber G
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1485-91 (2011)
PMID: 22139149

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

4 bound ligands:
Ligand SO4 1 x SO4
Ligand ACY 2 x ACY
Ligand MPD 3 x MPD
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P43212
Unit cell:
a: 128.538Å b: 128.538Å c: 103.865Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.224 0.272
Expression system: Escherichia coli

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Citations

1 mention without citation

Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy.
Tadwal et al. (2011)