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2zdi

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==Overview==
==Overview==
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Prefoldin (PFD) is a heterohexameric molecular chaperone complex in the, eukaryotic cytosol and archaea with a jellyfish-like structure containing, six long coiled-coil tentacles. PFDs capture protein folding intermediates, or unfolded polypeptides and transfer them to group II chaperonins for, facilitated folding. Although detailed studies on the mechanisms for, interaction with unfolded proteins or cooperation with chaperonins of, archaeal PFD have been performed, it is still unclear how PFD captures the, unfolded protein. In this study, we determined the X-ray structure of, Pyrococcus horikoshii OT3 PFD (PhPFD) at 3.0 A resolution and examined the, molecular mechanism for binding and recognition of nonnative substrate, proteins by molecular dynamics (MD) simulation and mutation analyses., PhPFD has a jellyfish-like structure with six long coiled-coil tentacles, and a large central cavity. Each subunit has a hydrophobic groove at the, distal region where an unfolded substrate protein is bound. During MD, simulation at 330 K, each coiled coil was highly flexible, enabling it to, widen its central cavity and capture various nonnative proteins. Docking, MD simulation of PhPFD with unfolded insulin showed that the beta subunit, is essentially involved in substrate binding and that the alpha subunit, modulates the shape and width of the central cavity. Analyses of mutant, PhPFDs with amino acid replacement of the hydrophobic residues of the beta, subunit in the hydrophobic groove have shown that betaIle107 has a, critical role in forming the hydrophobic groove.
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Prefoldin (PFD) is a heterohexameric molecular chaperone complex in the eukaryotic cytosol and archaea with a jellyfish-like structure containing six long coiled-coil tentacles. PFDs capture protein folding intermediates or unfolded polypeptides and transfer them to group II chaperonins for facilitated folding. Although detailed studies on the mechanisms for interaction with unfolded proteins or cooperation with chaperonins of archaeal PFD have been performed, it is still unclear how PFD captures the unfolded protein. In this study, we determined the X-ray structure of Pyrococcus horikoshii OT3 PFD (PhPFD) at 3.0 A resolution and examined the molecular mechanism for binding and recognition of nonnative substrate proteins by molecular dynamics (MD) simulation and mutation analyses. PhPFD has a jellyfish-like structure with six long coiled-coil tentacles and a large central cavity. Each subunit has a hydrophobic groove at the distal region where an unfolded substrate protein is bound. During MD simulation at 330 K, each coiled coil was highly flexible, enabling it to widen its central cavity and capture various nonnative proteins. Docking MD simulation of PhPFD with unfolded insulin showed that the beta subunit is essentially involved in substrate binding and that the alpha subunit modulates the shape and width of the central cavity. Analyses of mutant PhPFDs with amino acid replacement of the hydrophobic residues of the beta subunit in the hydrophobic groove have shown that betaIle107 has a critical role in forming the hydrophobic groove.
==About this Structure==
==About this Structure==
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[[Category: prefoldin]]
[[Category: prefoldin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:15:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:01:29 2008''

Revision as of 17:01, 21 February 2008

Image:2zdi.jpg

2zdi, resolution 3.0Å

Drag the structure with the mouse to rotate

Crystal structure of Prefoldin from Pyrococcus horikoshii OT3

Overview

Prefoldin (PFD) is a heterohexameric molecular chaperone complex in the eukaryotic cytosol and archaea with a jellyfish-like structure containing six long coiled-coil tentacles. PFDs capture protein folding intermediates or unfolded polypeptides and transfer them to group II chaperonins for facilitated folding. Although detailed studies on the mechanisms for interaction with unfolded proteins or cooperation with chaperonins of archaeal PFD have been performed, it is still unclear how PFD captures the unfolded protein. In this study, we determined the X-ray structure of Pyrococcus horikoshii OT3 PFD (PhPFD) at 3.0 A resolution and examined the molecular mechanism for binding and recognition of nonnative substrate proteins by molecular dynamics (MD) simulation and mutation analyses. PhPFD has a jellyfish-like structure with six long coiled-coil tentacles and a large central cavity. Each subunit has a hydrophobic groove at the distal region where an unfolded substrate protein is bound. During MD simulation at 330 K, each coiled coil was highly flexible, enabling it to widen its central cavity and capture various nonnative proteins. Docking MD simulation of PhPFD with unfolded insulin showed that the beta subunit is essentially involved in substrate binding and that the alpha subunit modulates the shape and width of the central cavity. Analyses of mutant PhPFDs with amino acid replacement of the hydrophobic residues of the beta subunit in the hydrophobic groove have shown that betaIle107 has a critical role in forming the hydrophobic groove.

About this Structure

2ZDI is a Protein complex structure of sequences from Pyrococcus horikoshii with as ligand. Full crystallographic information is available from OCA.

Reference

Structure and Molecular Dynamics Simulation of Archaeal Prefoldin: The Molecular Mechanism for Binding and Recognition of Nonnative Substrate Proteins., Ohtaki A, Kida H, Miyata Y, Ide N, Yonezawa A, Arakawa T, Iizuka R, Noguchi K, Kita A, Odaka M, Miki K, Yohda M, J Mol Biol. 2007 Dec 8;. PMID:18201719

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