1a6e
From Proteopedia
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| - | [[Image:1a6e.gif|left|200px]]<br /> | + | [[Image:1a6e.gif|left|200px]]<br /><applet load="1a6e" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a6e" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1a6e, resolution 3.2Å" /> | caption="1a6e, resolution 3.2Å" /> | ||
'''THERMOSOME-MG-ADP-ALF3 COMPLEX'''<br /> | '''THERMOSOME-MG-ADP-ALF3 COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A6E is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with MG, ADP and AF3 as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 1A6E is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with MG, ADP and AF3 as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=ASB:Residue Numbering According To Alpha-Type Subunit'>ASB</scene> and <scene name='pdbsite=ASE:Residue Numbering According To Alpha-Type Subunit'>ASE</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tric]] | [[Category: tric]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:10:01 2007'' |
Revision as of 12:00, 18 December 2007
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THERMOSOME-MG-ADP-ALF3 COMPLEX
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
1A6E is a Protein complex structure of sequences from Thermoplasma acidophilum with MG, ADP and AF3 as ligands. Known structural/functional Sites: and . 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 Tue Dec 18 14:10:01 2007
Categories: Protein complex | Thermoplasma acidophilum | Ditzel, L. | Huber, H. | Huber, R. | Loewe, J. | Steinbacher, S. | Stetter, K.O. | Stock, D. | ADP | AF3 | MG | Atp hydrolysis | Atpase | Cct | Group ii chaperonin | Protein folding | Transition state complex | Tric
