1dk7: Difference between revisions
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'''CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL''' | {{Structure | ||
|PDB= 1dk7 |SIZE=350|CAPTION= <scene name='initialview01'>1dk7</scene>, resolution 2.02Å | |||
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'''CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DK7 is a [ | 1DK7 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=1DK7 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10619429 10619429] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein folding]] | [[Category: protein folding]] | ||
''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 10:39:46 2008'' | ||
Revision as of 11:39, 20 March 2008
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CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL
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
1DK7 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
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