First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
1m5y
From Proteopedia
| 1m5y, resolution 3.00Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Gene: | sura (Escherichia coli) | ||||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding
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.
Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins., Bitto E, McKay DB, Structure. 2002 Nov;10(11):1489-98. PMID:12429090
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1m5y is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Bitto E, McKay DB. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure. 2002 Nov;10(11):1489-98. PMID:12429090
