1e0r

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(New page: 200px<br /><applet load="1e0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e0r, resolution 2.8&Aring;" /> '''BETA-APICAL DOMAIN OF...)
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[[Image:1e0r.jpg|left|200px]]<br /><applet load="1e0r" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1e0r, resolution 2.8&Aring;" />
'''BETA-APICAL DOMAIN OF THERMOSOME'''<br />
'''BETA-APICAL DOMAIN OF THERMOSOME'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E0R OCA].
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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.]]
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[[Category: Essen, L.O.]]
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[[Category: Essen, L O.]]
[[Category: chaperonin]]
[[Category: chaperonin]]
[[Category: groel]]
[[Category: groel]]
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[[Category: thermosome]]
[[Category: thermosome]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:43:05 2007''
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''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

Image:1e0r.jpg

1e0r, resolution 2.8Å

Drag the structure with the mouse to rotate

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

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