› 7w1d

X-ray diffraction
2.78Å resolution

Crystal structure of Klebsiella pneumoniae K1 capsule-specific polysaccharide lyase in a C2 crystal form

Released:
DOI: 10.2210/pdb7w1d/pdb
PDB entry 7w1d coloured by chain, front view.
PDB entry 7w1d coloured by chain, side view.
PDB entry 7w1d coloured by chain, top view.
Source organism: Klebsiella phage NTUH-K2044-K1-1
Primary publication:
Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use.
Tu IF, Lin TL, Yang FL, Lee IM, Tu WL, Liao JH, Ko TP, Wu WJ, Jan JT, Ho MR, Chou CY, Wang AH, Wu CY, Wang JT, Huang KF, Wu SH
J Biomed Sci 29 9 (2022)
PMID: 35130876

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Depolymerase, capsule K1-specific Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 671 amino acids
Theoretical weight: 72.13 KDa
Source organism: Klebsiella phage NTUH-K2044-K1-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A068Q5Q5 (Residues: 1-651; Coverage: 100%)
Gene name: ORF34

Ligands and Environments

2 bound ligands:
Ligand CIT 16 x CIT
Ligand CO3 3 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 363.945Å b: 239.626Å c: 121.632Å
α: 90° β: 100.13° γ: 90°
R-values:
R R work R free
0.184 0.182 0.219
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Potential of phage depolymerase for the treatment of bacterial biofilms.
Guo et al. (2023)
4 other articles

1 mention without citation

Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use.
Tu et al. (2022)