› 3htl

X-ray diffraction
1.8Å resolution

Structure of the Corynebacterium diphtheriae major pilin SpaA points to a modular pilus assembly with stabilizing isopeptide bonds

Released:
DOI: 10.2210/pdb3htl/pdb
PDB entry 3htl coloured by chain, front view.
PDB entry 3htl coloured by chain, side view.
PDB entry 3htl coloured by chain, top view.
Source organism: Corynebacterium diphtheriae
Primary publication:
The Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bonds.
Kang HJ, Paterson NG, Gaspar AH, Ton-That H, Baker EN
Proc Natl Acad Sci U S A 106 16967-71 (2009)
PMID: 19805181

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180030 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Surface-anchored fimbrial subunit Chain: X
Molecule details ›
Chain: X
Length: 436 amino acids
Theoretical weight: 47.07 KDa
Source organism: Corynebacterium diphtheriae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6NF81 (Residues: 53-486; Coverage: 87%)
Gene name: DIP2013
Sequence domains: Gram-positive pilin backbone subunit 2, Cna-B-like domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand NA 1 x NA
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P212121
Unit cell:
a: 34.78Å b: 64.037Å c: 199.192Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.19 0.242
Expression system: Escherichia coli BL21(DE3)

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Citations

16 review citations

Architects at the bacterial surface - sortases and the assembly of pili with isopeptide bonds.
Hendrickx et al. (2011)
15 more

7 mentions without citation

Structural biology of Gram-positive bacterial adhesins.
Vengadesan et al. (2011)
6 more