1a6d
From Proteopedia
(New page: 200px<br /><applet load="1a6d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a6d, resolution 2.6Å" /> '''THERMOSOME FROM T. AC...) |
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| - | [[Image:1a6d.gif|left|200px]]<br /><applet load="1a6d" size=" | + | [[Image:1a6d.gif|left|200px]]<br /><applet load="1a6d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a6d, resolution 2.6Å" /> | caption="1a6d, resolution 2.6Å" /> | ||
'''THERMOSOME FROM T. ACIDOPHILUM'''<br /> | '''THERMOSOME FROM T. ACIDOPHILUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined to 2.6 A resolution the crystal structure of the | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Loewe, J.]] | [[Category: Loewe, J.]] | ||
[[Category: Steinbacher, S.]] | [[Category: Steinbacher, S.]] | ||
| - | [[Category: Stetter, K | + | [[Category: Stetter, K O.]] |
[[Category: Stock, D.]] | [[Category: Stock, D.]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
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[[Category: tric]] | [[Category: tric]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:20 2008'' |
Revision as of 09:41, 21 February 2008
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THERMOSOME FROM T. ACIDOPHILUM
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.
About this Structure
1A6D is a Protein complex structure of sequences from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT., Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S, Cell. 1998 Apr 3;93(1):125-38. PMID:9546398
Page seeded by OCA on Thu Feb 21 11:41:20 2008
