1mnf
From Proteopedia
(New page: 200px<br /><applet load="1mnf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mnf, resolution 3.00Å" /> '''Domain motions in Gr...) |
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| - | [[Image:1mnf.gif|left|200px]]<br /><applet load="1mnf" size=" | + | [[Image:1mnf.gif|left|200px]]<br /><applet load="1mnf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mnf, resolution 3.00Å" /> | caption="1mnf, resolution 3.00Å" /> | ||
'''Domain motions in GroEL upon binding of an oligopeptide'''<br /> | '''Domain motions in GroEL upon binding of an oligopeptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | GroEL assists protein folding by preventing the interaction of partially | + | 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 Structure== | ==About this Structure== | ||
| - | 1MNF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1MNF is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: opposite allosteric]] | [[Category: opposite allosteric]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:02 2008'' |
Revision as of 11:57, 21 February 2008
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Domain motions in GroEL upon binding of an oligopeptide
Overview
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 Structure
1MNF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
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:14623189
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