› 1x1j

X-ray diffraction
2.1Å resolution

Crystal Structure of Xanthan Lyase (N194A) with a Substrate.

Released:
DOI: 10.2210/pdb1x1j/pdb
PDB entry 1x1j coloured by chain, front view.
PDB entry 1x1j coloured by chain, side view.
PDB entry 1x1j coloured by chain, top view.
Source organism: Bacillus sp. GL1
Primary publication:
Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism.
Maruyama Y, Hashimoto W, Mikami B, Murata K
J Mol Biol 350 974-86 (2005)
PMID: 15979090

Function and Biology Details

Reaction catalysed: 
Eliminative cleavage of the terminal beta-D-mannosyl-(1->4)-beta-D-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the side-chain
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189600 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xanthan lyase Chain: A
Molecule details ›
Chain: A
Length: 752 amino acids
Theoretical weight: 80.71 KDa
Source organism: Bacillus sp. GL1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9AQS0 (Residues: 26-777; Coverage: 83%)
Gene name: xly
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 46D 1 x 46D
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 53.747Å b: 90.026Å c: 74.249Å
α: 90° β: 91.06° γ: 90°
R-values:
R R work R free
0.179 0.179 0.236
Expression system: Escherichia coli

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Citations

2 review citations

Structural and mechanistic classification of uronic acid-containing polysaccharide lyases.
Garron et al. (2010)
1 more