2zdi
From Proteopedia
(New page: 200px<br /><applet load="2zdi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2zdi" /> ''''''<br /> ==About this Structure== is a [h...) |
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[[Image:2zdi.jpg|left|200px]]<br /><applet load="2zdi" size="350" color="white" frame="true" align="right" spinBox="true" | [[Image:2zdi.jpg|left|200px]]<br /><applet load="2zdi" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2zdi" /> | + | caption="2zdi, resolution 3.0Å" /> |
| - | ''''''<br /> | + | '''Crystal structure of Prefoldin from Pyrococcus horikoshii OT3'''<br /> |
| + | |||
| + | ==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== | ==About this Structure== | ||
| - | + | 2ZDI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZDI 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18201719 18201719] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| + | [[Category: Pyrococcus horikoshii]] | ||
| + | [[Category: Kida, H.]] | ||
| + | [[Category: Miki, K.]] | ||
| + | [[Category: SO4]] | ||
| + | [[Category: chaperone]] | ||
| + | [[Category: cytoplasm]] | ||
| + | [[Category: prefoldin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:25:17 2008'' |
Revision as of 15:25, 6 February 2008
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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
Page seeded by OCA on Wed Feb 6 17:25:17 2008
Categories: Protein complex | Pyrococcus horikoshii | Kida, H. | Miki, K. | SO4 | Chaperone | Cytoplasm | Prefoldin
