1aon

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1aon.jpg|left|200px]]
[[Image:1aon.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1aon |SIZE=350|CAPTION= <scene name='initialview01'>1aon</scene>, resolution 3.0&Aring;
+
The line below this paragraph, containing "STRUCTURE_1aon", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= GROE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1aon| PDB=1aon | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aon OCA], [http://www.ebi.ac.uk/pdbsum/1aon PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aon RCSB]</span>
+
-
}}
+
'''CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7'''
'''CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7'''
Line 29: Line 26:
[[Category: Sigler, P B.]]
[[Category: Sigler, P B.]]
[[Category: Xu, Z.]]
[[Category: Xu, Z.]]
-
[[Category: chaperonin assisted protein folding]]
+
[[Category: Chaperonin assisted protein folding]]
-
[[Category: complex (groel/groes)]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:31:20 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:44:31 2008''
+

Revision as of 07:31, 2 May 2008

Image:1aon.jpg


PDB ID 1aon

Drag the structure with the mouse to rotate
1aon, resolution 3.00Å ()
Ligands: ,
Gene: GROE (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
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 Page seeded by OCA on Fri May 2 10:31:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aon"
Personal tools