1a6d: Difference between revisions

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[[Image:1a6d.gif|left|200px]]<br /><applet load="1a6d" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1a6d.gif|left|200px]]<br /><applet load="1a6d" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1a6d, resolution 2.6Å" />

'''THERMOSOME FROM T. ACIDOPHILUM'''<br />

==Overview==

We have determined to 2.6 A resolution the crystal structure of the, thermosome, the archaeal group II chaperonin from T. acidophilum. The, hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an, (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to, GroEL but form a novel type of inter-ring contact. The domain arrangement, resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid, creating a closed conformation. The lid substitutes for a GroES-like, cochaperonin that is absent in the CCT/TRiC system. The central cavity has, a polar surface implicated in protein folding. Binding of the transition, state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds, to the ATP form.

We have determined to 2.6 A resolution the crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum. The hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to GroEL but form a novel type of inter-ring contact. The domain arrangement resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid creating a closed conformation. The lid substitutes for a GroES-like cochaperonin that is absent in the CCT/TRiC system. The central cavity has a polar surface implicated in protein folding. Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form.

==About this Structure==

1A6D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA].

1A6D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA].

==Reference==

Line 18:

[[Category: Loewe, J.]]

[[Category: Steinbacher, S.]]

[[Category: Stetter, K.O.]]

[[Category: Stetter, K O.]]

[[Category: Stock, D.]]

[[Category: atpase]]

Line 27:

[[Category: tric]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 10~~:38:~~19 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:20 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1a6d.gif|left|200px]]<br /><applet load="1a6d" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1a6d.gif|left|200px]]<br /><applet load="1a6d" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1a6d, resolution 2.6&Aring;" />
 '''THERMOSOME FROM T. ACIDOPHILUM'''<br />
 ==Overview==
-We have determined to 2.6 A resolution the crystal structure of the, thermosome, the archaeal group II chaperonin from T. acidophilum. The, hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an, (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to, GroEL but form a novel type of inter-ring contact. The domain arrangement, resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid, creating a closed conformation. The lid substitutes for a GroES-like, cochaperonin that is absent in the CCT/TRiC system. The central cavity has, a polar surface implicated in protein folding. Binding of the transition, state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds, to the ATP form.
+We have determined to 2.6 A resolution the crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum. The hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to GroEL but form a novel type of inter-ring contact. The domain arrangement resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid creating a closed conformation. The lid substitutes for a GroES-like cochaperonin that is absent in the CCT/TRiC system. The central cavity has a polar surface implicated in protein folding. Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form.
 ==About this Structure==
-A6D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA].
+A6D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: Loewe, J.]]
 [[Category: Steinbacher, S.]]
-[[Category: Stetter, K.O.]]
+[[Category: Stetter, K O.]]
 [[Category: Stock, D.]]
 [[Category: atpase]]
@@ Line 27: / Line 27: @@
 [[Category: tric]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:38:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:20 2008''