1mnf: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1mnf.gif|left|200px]]
[[Image:1mnf.gif|left|200px]]


{{Structure
<!--
|PDB= 1mnf |SIZE=350|CAPTION= <scene name='initialview01'>1mnf</scene>, resolution 3.00&Aring;
The line below this paragraph, containing "STRUCTURE_1mnf", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=  
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=
-->
|DOMAIN=
{{STRUCTURE_1mnf| PDB=1mnf  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mnf OCA], [http://www.ebi.ac.uk/pdbsum/1mnf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mnf RCSB]</span>
}}


'''Domain motions in GroEL upon binding of an oligopeptide'''
'''Domain motions in GroEL upon binding of an oligopeptide'''
Line 27: Line 24:
[[Category: Chen, L.]]
[[Category: Chen, L.]]
[[Category: Wang, J.]]
[[Category: Wang, J.]]
[[Category: domain motion]]
[[Category: Domain motion]]
[[Category: forced unfolding]]
[[Category: Forced unfolding]]
[[Category: groel]]
[[Category: Groel]]
[[Category: opposite allosteric]]
[[Category: Opposite allosteric]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:27:23 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:26 2008''

Revision as of 01:27, 3 May 2008

File:1mnf.gif

Template:STRUCTURE 1mnf

Domain motions in GroEL upon binding of an oligopeptide


OverviewOverview

GroEL assists protein folding by preventing the interaction of partially folded molecules with other non-native proteins. It binds them, sequesters them, and then releases them so that they can fold in an ATP-driven cycle. Previous studies have also shown that protein substrates, GroES, and oligopeptides bind to partially overlapped sites on the apical domain surfaces of GroEL. In this study, we have determined the crystal structure at 3.0A resolution of a symmetric (GroEL-peptide)(14) complex. The binding of each of these small 12 amino acid residue peptides to GroEL involves interactions between three adjacent apical domains of GroEL. Each peptide interacts primarily with a single GroEL subunit. Residues R231 and R268 from adjacent subunits isolate each substrate-binding pocket, and prevent bound substrates from sliding into adjacent binding pockets. As a consequence of peptide binding, domains rotate and inter-domain interactions are greatly enhanced. The direction of rotation of the apical domain of each GroEL subunit is opposite to that of its intermediate domain. Viewed from outside, the apical domains rotate clockwise within one GroEL ring, while the ATP-induced apical domain rotation is counter-clockwise.

About this StructureAbout this Structure

1MNF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Domain motions in GroEL upon binding of an oligopeptide., Wang J, Chen L, J Mol Biol. 2003 Nov 28;334(3):489-99. PMID:14623189 Page seeded by OCA on Sat May 3 01:27:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA