1dkd: Difference between revisions

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New page: left|200px<br /><applet load="1dkd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dkd, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1dkd.gif|left|200px]]<br /><applet load="1dkd" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dkd.gif|left|200px]]<br /><applet load="1dkd" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dkd, resolution 2.1&Aring;" />
caption="1dkd, resolution 2.1&Aring;" />
'''CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX'''<br />


==Overview==
==Overview==
The chaperonin GroEL is a double toriodal assembly that with its, cochaperonin GroES facilitates protein folding with an ATP-dependent, mechanism. Nonnative conformations of diverse protein substrates bind to, the apical domains surrounding the opening of the double toroid's central, cavity. Using phage display, we have selected peptides with high affinity, for the isolated apical domain. We have determined the crystal structures, of the complexes formed by the most strongly bound peptide with the, isolated apical domain, and with GroEL. The peptide interacts with the, groove between paired alpha helices in a manner similar to that of the, GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for, tight promiscuous binding of nonnative substrates and their release into, the shielded cis assembly.
The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, and with GroEL. The peptide interacts with the groove between paired alpha helices in a manner similar to that of the GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly.


==About this Structure==
==About this Structure==
1DKD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DKD OCA].  
1DKD 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=1DKD OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chen, L.]]
[[Category: Chen, L.]]
[[Category: Sigler, P.B.]]
[[Category: Sigler, P B.]]
[[Category: hsp60]]
[[Category: hsp60]]
[[Category: molecular chaperon]]
[[Category: molecular chaperon]]
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[[Category: protein folding]]
[[Category: protein folding]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:21:23 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:29 2008''

Revision as of 13:17, 21 February 2008

File:1dkd.gif


1dkd, resolution 2.1Å

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CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX

OverviewOverview

The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, and with GroEL. The peptide interacts with the groove between paired alpha helices in a manner similar to that of the GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly.

About this StructureAbout this Structure

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

ReferenceReference

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity., Chen L, Sigler PB, Cell. 1999 Dec 23;99(7):757-68. PMID:10619429

Page seeded by OCA on Thu Feb 21 12:17:29 2008

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