1mnf: Difference between revisions
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[[Image:1mnf.gif|left|200px]] | [[Image:1mnf.gif|left|200px]] | ||
'''Domain motions in GroEL upon binding of an oligopeptide''' | {{Structure | ||
|PDB= 1mnf |SIZE=350|CAPTION= <scene name='initialview01'>1mnf</scene>, resolution 3.00Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Domain motions in GroEL upon binding of an oligopeptide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MNF is a [ | 1MNF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNF OCA]. | ||
==Reference== | ==Reference== | ||
Domain motions in GroEL upon binding of an oligopeptide., Wang J, Chen L, J Mol Biol. 2003 Nov 28;334(3):489-99. PMID:[http:// | Domain motions in GroEL upon binding of an oligopeptide., Wang J, Chen L, J Mol Biol. 2003 Nov 28;334(3):489-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14623189 14623189] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: domain | [[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 Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:39 2008'' | ||
Revision as of 13:45, 20 March 2008
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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
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