1asx: Difference between revisions

Line 1:

[[Image:1asx.gif|left|200px]]<br /><applet load="1asx" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1asx.gif|left|200px]]<br /><applet load="1asx" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1asx, resolution 2.8Å" />

'''APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM'''<br />

==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.

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==

1ASX 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ASX OCA].

1ASX 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASX OCA].

==Reference==

Line 14:

[[Category: Thermoplasma acidophilum]]

[[Category: Baumeister, W.]]

[[Category: Essen, L.O.]]

[[Category: Essen, L O.]]

[[Category: Klumpp, M.]]

[[Category: PO4]]

Line 25:

[[Category: thermosome]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:06:~~56 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:03 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1asx.gif|left|200px]]<br /><applet load="1asx" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1asx.gif|left|200px]]<br /><applet load="1asx" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1asx, resolution 2.8&Aring;" />
 '''APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM'''<br />
 ==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.
+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==
-ASX 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ASX OCA].
+ASX 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASX OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Thermoplasma acidophilum]]
 [[Category: Baumeister, W.]]
-[[Category: Essen, L.O.]]
+[[Category: Essen, L O.]]
 [[Category: Klumpp, M.]]
 [[Category: PO4]]
@@ Line 25: / Line 25: @@
 [[Category: thermosome]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:06:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:03 2008''