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Structure paper

TitleThe Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues.
Journal, issue, pagesJ. Mol. Biol., Vol. 373, Page 367-381, Year 2007
Publish dateMay 9, 2007 (structure data deposition date)
AuthorsXu, X. / Wang, S. / Hu, Y.X. / McKay, D.B.
External linksJ. Mol. Biol. / PubMed:17825319
MethodsX-ray diffraction
Resolution1.3 - 3.39 Å
Structure data

PDB-2pv1:
Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide WEYIPNV
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-2pv2:
Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-2pv3:
Crystallographic Structure of SurA fragment lacking the second peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK
Method: X-RAY DIFFRACTION / Resolution: 3.39 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsISOMERASE / Survival protein A / Peptidyl-prolyl cis-trans isomerase domain / Complex

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