2c7c: Difference between revisions
New page: left|200px<br /><applet load="2c7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c7c" /> '''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO... |
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[[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" | ||
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'''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== | ||
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[[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]] | ||
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[[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 17:45, 21 February 2008
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FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)
OverviewOverview
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 StructureAbout this Structure
2C7C is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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