1aon
From Proteopedia
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| - | [[Image:1aon.jpg|left|200px]] | + | [[Image:1aon.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7''' | + | {{Structure |
| + | |PDB= 1aon |SIZE=350|CAPTION= <scene name='initialview01'>1aon</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= GROE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AON is a [ | + | 1AON is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1AON with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb32_1.html Chaperones]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AON OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex., Xu Z, Horwich AL, Sigler PB, Nature. 1997 Aug 21;388(6644):741-50. PMID:[http:// | + | The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex., Xu Z, Horwich AL, Sigler PB, Nature. 1997 Aug 21;388(6644):741-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9285585 9285585] |
[[Category: Chaperones]] | [[Category: Chaperones]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: complex (groel/groes)]] | [[Category: complex (groel/groes)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:21 2008'' |
Revision as of 08:00, 20 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | GROE (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7
Overview
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli, asymmetric intermediates of GroEL are formed with the co-chaperonin GroES and nucleotides bound only to one of the seven-subunit rings (the cis ring) and not to the opposing ring (the trans ring). The structure of the GroEL-GroES-(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and apical domains enable bound GroES to stabilize a folding chamber with ADP confined to the cis ring. Elevation and twist of the apical domains double the volume of the central cavity and bury hydrophobic peptide-binding residues in the interface with GroES, as well as between GroEL subunits, leaving a hydrophilic cavity lining that is conducive to protein folding. An inward tilt of the cis equatorial domain causes an outward tilt in the trans ring that opposes the binding of a second GroES. When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid.
About this Structure
1AON is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 1AON with [Chaperones]. Full crystallographic information is available from OCA.
Reference
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex., Xu Z, Horwich AL, Sigler PB, Nature. 1997 Aug 21;388(6644):741-50. PMID:9285585
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