› 3k8m

X-ray diffraction
2.5Å resolution

Crystal structure of SusG with acarbose

Released:
DOI: 10.2210/pdb3k8m/pdb
PDB entry 3k8m coloured by chain, front view.
PDB entry 3k8m coloured by chain, side view.
PDB entry 3k8m coloured by chain, top view.
Source organism: Bacteroides thetaiotaomicron
Primary publication:
SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules.
Koropatkin NM, Smith TJ
Structure 18 200-15 (2010)
PMID: 20159465

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Alpha-amylase SusG Chains: A, B
Molecule details ›
Chains: A, B
Length: 669 amino acids
Theoretical weight: 75.83 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A1G3 (Residues: 24-692; Coverage: 100%)
Gene names: BT_3698, susG
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, AC1
Ligand GLC 2 x GLC
Ligand AC1 2 x AC1
Carbohydrate polymer : NEW Components: GLC, AC1
Ligand GLC 8 x GLC
Ligand AC1 4 x AC1
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand CA 4 x CA
Ligand EDO 1 x EDO
1 modified residue:
Ligand MSE 22 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41
Unit cell:
a: 127.709Å b: 127.709Å c: 127.987Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.247
Expression system: Escherichia coli

Quick links

Citations

21 review citations

How glycan metabolism shapes the human gut microbiota.
Koropatkin et al. (2012)
20 more

1 mention without citation

Modulating Glycoside Hydrolase Activity between Hydrolysis and Transfer Reactions Using an Evolutionary Approach.
Arreola-Barroso et al. (2021)