› 1c5h

X-ray diffraction
1.55Å resolution

HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE

Released:
DOI: 10.2210/pdb1c5h/pdb
PDB entry 1c5h coloured by chain, front view.
PDB entry 1c5h coloured by chain, side view.
PDB entry 1c5h coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase.
Joshi MD, Sidhu G, Pot I, Brayer GD, Withers SG, McIntosh LP
J Mol Biol 299 255-79 (2000)
PMID: 10860737

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140770 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.41 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P09850 (Residues: 29-213; Coverage: 100%)
Gene name: xlnA
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 44.05Å b: 52.69Å c: 78.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 not available
Expression system: Escherichia coli BL21

Quick links

Citations

11 review citations

Xylanases, xylanase families and extremophilic xylanases.
Collins et al. (2005)
10 more

3 mentions without citation

Relating destabilizing regions to known functional sites in proteins.
Dessailly et al. (2007)
2 more