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1e0r
From Proteopedia
(New page: 200px<br /><applet load="1e0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e0r, resolution 2.8Å" /> '''BETA-APICAL DOMAIN OF...) |
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| - | [[Image:1e0r.jpg|left|200px]]<br /><applet load="1e0r" size=" | + | [[Image:1e0r.jpg|left|200px]]<br /><applet load="1e0r" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e0r, resolution 2.8Å" /> | caption="1e0r, resolution 2.8Å" /> | ||
'''BETA-APICAL DOMAIN OF THERMOSOME'''<br /> | '''BETA-APICAL DOMAIN OF THERMOSOME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the beta-apical domain of the thermosome, an | + | The crystal structure of the beta-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 A resolution. The structure shows an invariant globular core from which a 25 A long protrusion emanates, composed of an elongated alpha-helix (H10) and a long extended stretch consisting of residues GluB245-ThrB253. A comparison with previous apical domain structures reveals a large segmental displacement of the protruding part of helix H10 via the hinge GluB276-ValB278. The region comprising residues GluB245-ThrB253 adopts an extended beta-like conformation rather than the alpha-helix seen in the alpha-apical domain. Consequently, it appears that the protrusions of the apical domains from group II chaperonins might assume a variety of context-dependent conformations during an open, substrate-accepting state of the chaperonin. Sequence variations in the protrusion regions that are found in the eukaryotic TRiC/CCT subunits may provide different structural propensities and hence serve different roles in substrate recognition. |
==About this Structure== | ==About this Structure== | ||
| - | 1E0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http:// | + | 1E0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1E0R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Baumeister, W.]] | [[Category: Baumeister, W.]] | ||
[[Category: Bosch, G.]] | [[Category: Bosch, G.]] | ||
| - | [[Category: Essen, L | + | [[Category: Essen, L O.]] |
[[Category: chaperonin]] | [[Category: chaperonin]] | ||
[[Category: groel]] | [[Category: groel]] | ||
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[[Category: thermosome]] | [[Category: thermosome]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:34 2008'' |
Revision as of 10:22, 21 February 2008
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BETA-APICAL DOMAIN OF THERMOSOME
Overview
The crystal structure of the beta-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 A resolution. The structure shows an invariant globular core from which a 25 A long protrusion emanates, composed of an elongated alpha-helix (H10) and a long extended stretch consisting of residues GluB245-ThrB253. A comparison with previous apical domain structures reveals a large segmental displacement of the protruding part of helix H10 via the hinge GluB276-ValB278. The region comprising residues GluB245-ThrB253 adopts an extended beta-like conformation rather than the alpha-helix seen in the alpha-apical domain. Consequently, it appears that the protrusions of the apical domains from group II chaperonins might assume a variety of context-dependent conformations during an open, substrate-accepting state of the chaperonin. Sequence variations in the protrusion regions that are found in the eukaryotic TRiC/CCT subunits may provide different structural propensities and hence serve different roles in substrate recognition.
About this Structure
1E0R is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region., Bosch G, Baumeister W, Essen LO, J Mol Biol. 2000 Aug 4;301(1):19-25. PMID:10926489
Page seeded by OCA on Thu Feb 21 12:22:34 2008
Categories: Single protein | Thermoplasma acidophilum | Baumeister, W. | Bosch, G. | Essen, L O. | Chaperonin | Groel | Hsp60 | Tcp1 | Thermosome
