› 4awd

X-ray diffraction
2.4Å resolution

Crystal structure of the beta-porphyranase BpGH16B (BACPLE_01689) from the human gut bacterium Bacteroides plebeius

Released:
DOI: 10.2210/pdb4awd/pdb
PDB entry 4awd coloured by chain, front view.
PDB entry 4awd coloured by chain, side view.
PDB entry 4awd coloured by chain, top view.
Source organism: Phocaeicola plebeius
Primary publication:
Bacteria of the human gut microbiome catabolize red seaweed glycans with carbohydrate-active enzyme updates from extrinsic microbes.
Hehemann JH, Kelly AG, Pudlo NA, Martens EC, Boraston AB
Proc Natl Acad Sci U S A 109 19786-91 (2012)
PMID: 23150581

Function and Biology Details

Reaction catalysed: 
Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110187 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-porphyranase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 324 amino acids
Theoretical weight: 37.52 KDa
Source organism: Phocaeicola plebeius
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B5CY92 (Residues: 21-321; Coverage: 100%)
Gene name: BACPLE_01689
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Unit cell:
a: 51.12Å b: 107.23Å c: 137.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.25
Expression system: Escherichia coli BL21(DE3)

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Citations

34 review citations

The abundance and variety of carbohydrate-active enzymes in the human gut microbiota.
El Kaoutari et al. (2013)
33 more

4 mentions without citation

Bacteria of the human gut microbiome catabolize red seaweed glycans with carbohydrate-active enzyme updates from extrinsic microbes.
Hehemann et al. (2012)
3 more