1jon
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1jon.jpg|left|200px]] | [[Image:1jon.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1jon", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_1jon| PDB=1jon | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345''' | '''GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345''' | ||
| Line 27: | Line 24: | ||
[[Category: Buckle, A M.]] | [[Category: Buckle, A M.]] | ||
[[Category: Fersht, A R.]] | [[Category: Fersht, A R.]] | ||
| - | [[Category: | + | [[Category: Atp-binding]] |
| - | [[Category: | + | [[Category: Cell division]] |
| - | [[Category: | + | [[Category: Chaperone]] |
| - | [[Category: | + | [[Category: Phosphorylation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:31:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:31, 2 May 2008
GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345
Overview
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and cyclophilin A in the absence of ATP and in catalyzing the unfolding of native barnase. Its crystal structure, solved at 2.5 A resolution, shows a well-ordered domain with the same fold as in intact GroEL. We have thus isolated the active site of the complex allosteric molecular chaperone, which functions as a "minichaperone." This has mechanistic implications: the presence of a central cavity in the GroEL complex is not essential for those representative activities in vitro, and neither are the allosteric properties. The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions.
About this Structure
1JON is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL., Zahn R, Buckle AM, Perrett S, Johnson CM, Corrales FJ, Golbik R, Fersht AR, Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15024-9. PMID:8986757 Page seeded by OCA on Fri May 2 21:31:08 2008
