› 3mam

X-ray diffraction
1.8Å resolution

A molecular switch changes the low to the high affinity state in the substrate binding protein AfProX

Released:
DOI: 10.2210/pdb3mam/pdb
PDB entry 3mam coloured by chain, front view.
PDB entry 3mam coloured by chain, side view.
PDB entry 3mam coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state.
Tschapek B, Pittelkow M, Sohn-Bösser L, Holtmann G, Smits SH, Gohlke H, Bremer E, Schmitt L
J Mol Biol 411 36-52 (2011)
PMID: 21664363

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-128106 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ABC-type glycine betaine transport system substrate-binding domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 30.59 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O29280 (Residues: 23-292; Coverage: 93%)
Gene name: AF_0982
Sequence domains: Substrate binding domain of ABC-type glycine betaine transport system
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand BET 1 x BET
Ligand EDO 7 x EDO
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P1
Unit cell:
a: 33.792Å b: 36.958Å c: 57.886Å
α: 96.07° β: 99.57° γ: 96.12°
R-values:
R R work R free
0.204 0.202 0.247
Expression system: Escherichia coli

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Citations

1 review citation

Role of the Extremolytes Ectoine and Hydroxyectoine as Stress Protectants and Nutrients: Genetics, Phylogenomics, Biochemistry, and Structural Analysis.
Czech et al. (2018)
12 other articles