› 2pv2

X-ray diffraction
1.3Å resolution

Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK

Released:
DOI: 10.2210/pdb2pv2/pdb
PDB entry 2pv2 coloured by chain, front view.
PDB entry 2pv2 coloured by chain, side view.
PDB entry 2pv2 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 domain:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142222 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone SurA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 103 amino acids
Theoretical weight: 10.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ABZ6 (Residues: 172-274; Coverage: 25%)
Gene names: JW0052, b0053, surA
Sequence domains: PPIC-type PPIASE domain
Structure domains: Chitinase A; domain 3
C-peptide Chains: E, F
Molecule details ›
Chains: E, F
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: P21
Unit cell:
a: 56.46Å b: 50.63Å c: 74.06Å
α: 90° β: 111.54° γ: 90°
R-values:
R R work R free
0.208 0.208 0.227
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

4 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)
3 more