› 2ntp

X-ray diffraction
1.7Å resolution

Crystal structure of pectin methylesterase in complex with hexasaccharide VI

Released:
DOI: 10.2210/pdb2ntp/pdb
PDB entry 2ntp coloured by chain, front view.
PDB entry 2ntp coloured by chain, side view.
PDB entry 2ntp coloured by chain, top view.
Source organism: Dickeya dadantii 3937
Primary publication:
Molecular basis of the activity of the phytopathogen pectin methylesterase.
Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW
EMBO J 26 3879-87 (2007)
PMID: 17717531

Function and Biology Details

Reaction catalysed: 
Pectin + n H(2)O = n methanol + pectate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Pectinesterase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 36.99 KDa
Source organism: Dickeya dadantii 3937
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C1A9 (Residues: 25-366; Coverage: 100%)
Gene names: Dda3937_03374, pem, pemA
Sequence domains: Pectinesterase
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: ADA, M8C
Carbohydrate polymer
Carbohydrate polymer : NEW Components: ADA, SHB
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P21
Unit cell:
a: 51.091Å b: 85Å c: 97.325Å
α: 90° β: 93.56° γ: 90°
R-values:
R R work R free
0.186 0.184 0.217
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The biochemistry and structural biology of plant cell wall deconstruction.
Gilbert HJ. (2010)
4 more

5 mentions without citation

Structural biology of pectin degradation by Enterobacteriaceae.
Abbott et al. (2008)
4 more