1ass

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(New page: 200px<br /><applet load="1ass" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ass, resolution 2.3&Aring;" /> '''APICAL DOMAIN OF THE ...)
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[[Image:1ass.gif|left|200px]]<br /><applet load="1ass" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ass.gif|left|200px]]<br /><applet load="1ass" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ass, resolution 2.3&Aring;" />
caption="1ass, resolution 2.3&Aring;" />
'''APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM'''<br />
'''APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM'''<br />
==Overview==
==Overview==
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The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution., The core resembles the apical domain of GroEL but lacks the hydrophobic, residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix, motif, which is characteristic of all group II chaperonins including the, eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are, consistent with cryo electron microscopy data, suggest a dual role of this, helical protrusion in substrate binding and controlling access to the, central cavity independent of a GroES-like cochaperonin.
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The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution. The core resembles the apical domain of GroEL but lacks the hydrophobic residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix motif, which is characteristic of all group II chaperonins including the eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are consistent with cryo electron microscopy data, suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaperonin.
==About this Structure==
==About this Structure==
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1ASS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with NA and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ASS OCA].
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1ASS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASS OCA].
==Reference==
==Reference==
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[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Baumeister, W.]]
[[Category: Baumeister, W.]]
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[[Category: Essen, L.O.]]
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[[Category: Essen, L O.]]
[[Category: Klumpp, M.]]
[[Category: Klumpp, M.]]
[[Category: NA]]
[[Category: NA]]
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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 11:06:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:58 2008''

Revision as of 09:48, 21 February 2008

Image:1ass.gif

1ass, resolution 2.3Å

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APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM

Overview

The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution. The core resembles the apical domain of GroEL but lacks the hydrophobic residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix motif, which is characteristic of all group II chaperonins including the eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are consistent with cryo electron microscopy data, suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaperonin.

About this Structure

1ASS is a Single protein structure of sequence from Thermoplasma acidophilum with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin., Klumpp M, Baumeister W, Essen LO, Cell. 1997 Oct 17;91(2):263-70. PMID:9346243

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