1fxk: Difference between revisions

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==Overview==

Prefoldin (GimC) is a hexameric molecular chaperone complex built from two, related classes of subunits and present in all eukaryotes and archaea., Prefoldin interacts with nascent polypeptide chains and, in vitro, can, functionally substitute for the Hsp70 chaperone system in stabilizing, non-native proteins for subsequent folding in the central cavity of a, chaperonin. Here, we present the crystal structure and characterization of, the prefoldin hexamer from the archaeum Methanobacterium, thermoautotrophicum. Prefoldin has the appearance of a jellyfish: its body, consists of a double beta barrel assembly with six long tentacle-like, coiled coils protruding from it. The distal regions of the coiled coils, expose hydrophobic patches and are required for multivalent binding of, nonnative proteins.

Prefoldin (GimC) is a hexameric molecular chaperone complex built from two related classes of subunits and present in all eukaryotes and archaea. Prefoldin interacts with nascent polypeptide chains and, in vitro, can functionally substitute for the Hsp70 chaperone system in stabilizing non-native proteins for subsequent folding in the central cavity of a chaperonin. Here, we present the crystal structure and characterization of the prefoldin hexamer from the archaeum Methanobacterium thermoautotrophicum. Prefoldin has the appearance of a jellyfish: its body consists of a double beta barrel assembly with six long tentacle-like coiled coils protruding from it. The distal regions of the coiled coils expose hydrophobic patches and are required for multivalent binding of nonnative proteins.

==About this Structure==

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[[Category: archaeal protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:49~~:37~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:49 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Prefoldin (GimC) is a hexameric molecular chaperone complex built from two, related classes of subunits and present in all eukaryotes and archaea., Prefoldin interacts with nascent polypeptide chains and, in vitro, can, functionally substitute for the Hsp70 chaperone system in stabilizing, non-native proteins for subsequent folding in the central cavity of a, chaperonin. Here, we present the crystal structure and characterization of, the prefoldin hexamer from the archaeum Methanobacterium, thermoautotrophicum. Prefoldin has the appearance of a jellyfish: its body, consists of a double beta barrel assembly with six long tentacle-like, coiled coils protruding from it. The distal regions of the coiled coils, expose hydrophobic patches and are required for multivalent binding of, nonnative proteins.
+Prefoldin (GimC) is a hexameric molecular chaperone complex built from two related classes of subunits and present in all eukaryotes and archaea. Prefoldin interacts with nascent polypeptide chains and, in vitro, can functionally substitute for the Hsp70 chaperone system in stabilizing non-native proteins for subsequent folding in the central cavity of a chaperonin. Here, we present the crystal structure and characterization of the prefoldin hexamer from the archaeum Methanobacterium thermoautotrophicum. Prefoldin has the appearance of a jellyfish: its body consists of a double beta barrel assembly with six long tentacle-like coiled coils protruding from it. The distal regions of the coiled coils expose hydrophobic patches and are required for multivalent binding of nonnative proteins.
 ==About this Structure==
@@ Line 19: / Line 19: @@
 [[Category: archaeal protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:49:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:49 2008''