1dkd
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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
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