1M5Y
Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding
Summary for 1M5Y
| Entry DOI | 10.2210/pdb1m5y/pdb |
| Descriptor | Survival protein surA (1 entity in total) |
| Functional Keywords | survival protein a, periplasmic molecular chaperone, membrane protein folding, gram negative bacteria, isomerase, cell cycle |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 180527.70 |
| Authors | Bitto, E.,McKay, D.B. (deposition date: 2002-07-10, release date: 2002-11-08, Last modification date: 2024-02-14) |
| Primary citation | Bitto, E.,McKay, D.B. Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Folding of Outer Membrane Porins Structure, 10:1489-1498, 2002 Cited by PubMed Abstract: The SurA protein facilitates correct folding of outer membrane proteins in gram-negative bacteria. The sequence of Escherichia coli SurA presents four segments, two of which are peptidyl-prolyl isomerases (PPIases); the crystal structure reveals an asymmetric dumbbell, in which the amino-terminal, carboxy-terminal, and first PPIase segments of the sequence form a core structural module, and the second PPIase segment is a satellite domain tethered approximately 30 A from this module. The core module, which is implicated in membrane protein folding, has a novel fold that includes an extended crevice. Crystal contacts show that peptides bind within the crevice, suggesting a model for chaperone activity whereby segments of polypeptide may be repetitively sequestered and released during the membrane protein-folding process. PubMed: 12429090DOI: 10.1016/S0969-2126(02)00877-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
