› 4cn4

X-ray diffraction
2.4Å resolution

GlgE isoform 1 from Streptomyces coelicolor E423A mutant with 2-deoxy- 2-fluoro-beta-maltosyl modification

Released:
DOI: 10.2210/pdb4cn4/pdb
PDB entry 4cn4 coloured by chain, front view.
PDB entry 4cn4 coloured by chain, side view.
PDB entry 4cn4 coloured by chain, top view.
Source organism: Streptomyces coelicolor
Primary publication:
Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate.
Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S
Biochemistry 53 2494-504 (2014)
PMID: 24689960

Function and Biology Details

Reaction catalysed: 
Alpha-maltose 1-phosphate + ((1->4)-alpha-D-glucosyl)(n) = phosphate + ((1->4)-alpha-D-glucosyl)(n+2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 695 amino acids
Theoretical weight: 77.51 KDa
Source organism: Streptomyces coelicolor
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L1K2 (Residues: 1-675; Coverage: 100%)
Gene names: SC6A11.19c, SCO5443, glgE1, pep1, pep1A, pep1I
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: SHG, GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P41212
Unit cell:
a: 113Å b: 113Å c: 312.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.208
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Diversity of phosphorylases in glycoside hydrolase families.
Kitaoka M. (2015)
4 more

2 mentions without citation

Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate.
Syson et al. (2014)
1 more