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.
1gr5
From Proteopedia
| 1gr5, resolution 7.90Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Related: | 1aon, 1der, 1fy9, 1fya, 1grl, 1jon, 1kid, 1oel, 2c7e, 1gru | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Solution Structure of apo GroEL by Cryo-Electron microscopy
The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines.
ATP-bound states of GroEL captured by cryo-electron microscopy., Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR, Cell. 2001 Dec 28;107(7):869-79. PMID:11779463
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1gr5 is a 14 chain structure of Chaperonin and Heat Shock Proteins with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR. ATP-bound states of GroEL captured by cryo-electron microscopy. Cell. 2001 Dec 28;107(7):869-79. PMID:11779463
- Xu Z, Horwich AL, Sigler PB. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 1997 Aug 21;388(6644):741-50. PMID:9285585 doi:10.1038/41944
- Boisvert DC, Wang J, Otwinowski Z, Horwich AL, Sigler PB. The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. Nat Struct Biol. 1996 Feb;3(2):170-7. PMID:8564544
- Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB. The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature. 1994 Oct 13;371(6498):578-86. PMID:7935790 doi:10.1038/371578a0
