2c7e
From Proteopedia
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[[Image:2c7e.gif|left|200px]] | [[Image:2c7e.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_2c7e| PDB=2c7e | SCENE= }} | |
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'''REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)''' | '''REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2C7E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry | + | 2C7E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gr6 1gr6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Roseman, A M.]] | [[Category: Roseman, A M.]] | ||
[[Category: Saibil, H R.]] | [[Category: Saibil, H R.]] | ||
| - | [[Category: | + | [[Category: Atp]] |
| - | [[Category: | + | [[Category: Atp-binding]] |
| - | [[Category: | + | [[Category: Cell cycle]] |
| - | [[Category: | + | [[Category: Cell division]] |
| - | [[Category: | + | [[Category: Chaperone]] |
| - | [[Category: | + | [[Category: Chaperonin]] |
| - | [[Category: | + | [[Category: D398a]] |
| - | [[Category: | + | [[Category: Hp60 class]] |
| - | [[Category: | + | [[Category: Nucleotide-binding]] |
| - | [[Category: | + | [[Category: Phosphorylation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:22:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:22, 3 May 2008
REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)
Overview
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.
About this Structure
2C7E is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1gr6. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 21:22:42 2008
