View source for 1aon

[[Image:1aon.jpg|left|200px]]

 {{Structure
|PDB= 1aon |SIZE=350|CAPTION= <scene name='initialview01'>1aon</scene>, resolution 3.0&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5&#39;-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==
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 [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==
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: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Horwich, A L.]]
[[Category: Sigler, P B.]]
[[Category: Xu, Z.]]
[[Category: ADP]]
[[Category: MG]]
[[Category: chaperonin assisted protein folding]]
[[Category: complex (groel/groes)]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:08:56 2008''