This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2c7c
From Proteopedia
(New page: 200px<br /><applet load="2c7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c7c" /> '''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2c7c.gif|left|200px]]<br /><applet load="2c7c" size=" | + | [[Image:2c7c.gif|left|200px]]<br /><applet load="2c7c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2c7c" /> | caption="2c7c" /> | ||
'''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)'''<br /> | '''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form | + | The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein. |
==About this Structure== | ==About this Structure== | ||
| - | 2C7C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 2C7C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7C OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Clare, D | + | [[Category: Clare, D K.]] |
| - | [[Category: Farr, G | + | [[Category: Farr, G W.]] |
| - | [[Category: Horwich, A | + | [[Category: Horwich, A L.]] |
[[Category: Houldershaw, D.]] | [[Category: Houldershaw, D.]] | ||
| - | [[Category: Ranson, N | + | [[Category: Ranson, N A.]] |
| - | [[Category: Saibil, H | + | [[Category: Saibil, H R.]] |
[[Category: atomic structure fitting]] | [[Category: atomic structure fitting]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
| Line 28: | Line 28: | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:42 2008'' |
Revision as of 14:45, 21 February 2008
|
FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)
Overview
The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.
About this Structure
2C7C is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes., Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR, Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:16429154
Page seeded by OCA on Thu Feb 21 16:45:42 2008
