› 3k02

X-ray diffraction
1.55Å resolution

Crystal structures of the GacH receptor of Streptomyces glaucescens GLA.O in the unliganded form and in complex with acarbose and an acarbose homolog. Comparison with acarbose-loaded maltose binding protein of Salmonella typhimurium.

Released:
DOI: 10.2210/pdb3k02/pdb
PDB entry 3k02 coloured by chain, front view.
PDB entry 3k02 coloured by chain, side view.
PDB entry 3k02 coloured by chain, top view.
Source organism: Streptomyces glaucescens
Primary publication:
Crystal structures of the solute receptor GacH of Streptomyces glaucescens in complex with acarbose and an acarbose homolog: comparison with the acarbose-loaded maltose-binding protein of Salmonella typhimurium.
Vahedi-Faridi A, Licht A, Bulut H, Scheffel F, Keller S, Wehmeier UF, Saenger W, Schneider E
J Mol Biol 397 709-23 (2010)
PMID: 20132828

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-109104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acarbose/maltose binding protein Chain: A
Molecule details ›
Chain: A
Length: 409 amino acids
Theoretical weight: 43.96 KDa
Source organism: Streptomyces glaucescens
Expression system: Escherichia coli
UniProt:
  • Canonical: B0B0V1 (Residues: 37-424; Coverage: 96%)
Gene names: SGLAU_00965, gacH
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand TXT 1 x TXT
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P41212
Unit cell:
a: 72.177Å b: 72.177Å c: 160.454Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.243
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
Eitinger et al. (2011)
1 more