› 2pv3

X-ray diffraction
3.39Å resolution

Crystallographic Structure of SurA fragment lacking the second peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK

Released:
DOI: 10.2210/pdb2pv3/pdb
PDB entry 2pv3 coloured by chain, front view.
PDB entry 2pv3 coloured by chain, side view.
PDB entry 2pv3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.
Xu X, Wang S, Hu YX, McKay DB
J Mol Biol 373 367-81 (2007)
PMID: 17825319

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142223 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone SurA Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 33.22 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ABZ6 (Residues: 21-428; Coverage: 73%)
Gene names: JW0052, b0053, surA
Sequence domains:
Structure domains:
C-peptide Chain: C
Molecule details ›
Chain: C
Length: 12 amino acids
Theoretical weight: 1.62 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P3221
Unit cell:
a: 148.33Å b: 148.33Å c: 188.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.284 0.284 0.299
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

18 review citations

β-Barrel membrane protein assembly by the Bam complex.
Hagan et al. (2011)
17 more

7 mentions without citation

The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.
Xu et al. (2007)
6 more