1fxk: Difference between revisions

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[[Image:1fxk.~~jpg~~|left|200px]]

[[Image:1fxk.png|left|200px]]

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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.

==About this Structure==

The following page contains interesting information on the relation of 1FXK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb32_1.html Chaperones]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXK OCA].

~~==Reference==~~

Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins., Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I, Cell. 2000 Nov 10;103(4):621-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106732 11106732]

[[Category: Chaperones]]

[[Category: Moarefi, I.]]

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[[Category: Siegert, R.]]

[[Category: Archaeal protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 16~~:52:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:23:51 2008''

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-[[Image:1fxk.jpg|left|200px]]
+[[Image:1fxk.png|left|200px]]
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-==Overview==
+{{ABSTRACT_11106732}}
-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==
 The following page contains interesting information on the relation of 1FXK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb32_1.html Chaperones]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXK OCA].
-==Reference==
-Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins., Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I, Cell. 2000 Nov 10;103(4):621-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106732 11106732]
 [[Category: Chaperones]]
 [[Category: Moarefi, I.]]
@@ Line 25: / Line 21: @@
 [[Category: Siegert, R.]]
 [[Category: Archaeal protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:52:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:23:51 2008''