› 4tsm

X-ray diffraction
1.9Å resolution

MBP-fusion protein of PilA1 from C. difficile R20291 residues 26-166

Released:
DOI: 10.2210/pdb4tsm/pdb
PDB entry 4tsm coloured by chain, front view.
PDB entry 4tsm coloured by chain, side view.
PDB entry 4tsm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and evolutionary analyses show unique stabilization strategies in the type IV pili of Clostridium difficile.
Piepenbrink KH, Maldarelli GA, Martinez de la Peña CF, Dingle TC, Mulvey GL, Lee A, von Rosenvinge E, Armstrong GD, Donnenberg MS, Sundberg EJ
Structure 23 385-96 (2015)
PMID: 25599642

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltose/maltodextrin-binding periplasmic protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 520 amino acids
Theoretical weight: 56.38 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand TMO 19 x TMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 143.951Å b: 79.366Å c: 164.746Å
α: 90° β: 90.23° γ: 90°
R-values:
R R work R free
0.197 0.197 0.233
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Motility and adhesion through type IV pili in Gram-positive bacteria.
Piepenbrink et al. (2016)
7 more

3 mentions without citation

Crystal structures of MBP fusion proteins.
Waugh DS. (2016)
2 more