› 4pmu

X-ray diffraction
2.86Å resolution

Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211)

Released:
DOI: 10.2210/pdb4pmu/pdb
PDB entry 4pmu coloured by chain, front view.
PDB entry 4pmu coloured by chain, side view.
PDB entry 4pmu coloured by chain, top view.
Source organism: Xanthomonas citri pv. citri str. 306
Primary publication:
Molecular mechanisms associated with xylan degradation by Xanthomonas plant pathogens.
Santos CR, Hoffmam ZB, de Matos Martins VP, Zanphorlin LM, de Paula Assis LH, Honorato RV, Lopes de Oliveira PS, Ruller R, Murakami MT
J Biol Chem 289 32186-32200 (2014)
PMID: 25266726

Function and Biology Details

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-241390 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase A Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 356 amino acids
Theoretical weight: 39.84 KDa
Source organism: Xanthomonas citri pv. citri str. 306
Expression system: Escherichia coli BL21(DE3)
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P21
Unit cell:
a: 87.022Å b: 100.741Å c: 134.199Å
α: 90° β: 95.15° γ: 90°
R-values:
R R work R free
0.213 0.211 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation.
Malgas et al. (2019)
1 more

1 mention without citation

Molecular mechanisms associated with xylan degradation by Xanthomonas plant pathogens.
Santos et al. (2014)