1do2: Difference between revisions

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[[Image:1do2.gif|left|200px]]<br /><applet load="1do2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1do2.gif|left|200px]]<br /><applet load="1do2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1do2, resolution 4.00Å" />

'''TRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI'''<br />

==Overview==

The degradation of cytoplasmic proteins is an ATP-dependent process., Substrates are targeted to a single soluble protease, the 26S proteasome, in eukaryotes and to a number of unrelated proteases in prokaryotes. A, surprising link emerged with the discovery of the ATP-dependent protease, HslVU (heat shock locus VU) in Escherichia coli. Its protease component, HslV shares approximately 20% sequence similarity and a conserved fold, with 20S proteasome beta-subunits. HslU is a member of the Hsp100 (Clp), family of ATPases. Here we report the crystal structures of free HslU and, an 820,000 relative molecular mass complex of HslU and HslV-the first, structure of a complete set of components of an ATP-dependent protease., HslV and HslU display sixfold symmetry, ruling out mechanisms of protease, activation that require a symmetry mismatch between the two components., Instead, there is conformational flexibility and domain motion in HslU and, a localized order-disorder transition in HslV. Individual subunits of HslU, contain two globular domains in relative orientations that correlate with, nucleotide bound and unbound states. They are surprisingly similar to, their counterparts in N-ethylmaleimide-sensitive fusion protein, the, prototype of an AAA-ATPase. A third, mostly alpha-helical domain in HslU, mediates the contact with HslV and may be the structural equivalent of the, amino-terminal domains in proteasomal AAA-ATPases.

The degradation of cytoplasmic proteins is an ATP-dependent process. Substrates are targeted to a single soluble protease, the 26S proteasome, in eukaryotes and to a number of unrelated proteases in prokaryotes. A surprising link emerged with the discovery of the ATP-dependent protease HslVU (heat shock locus VU) in Escherichia coli. Its protease component HslV shares approximately 20% sequence similarity and a conserved fold with 20S proteasome beta-subunits. HslU is a member of the Hsp100 (Clp) family of ATPases. Here we report the crystal structures of free HslU and an 820,000 relative molecular mass complex of HslU and HslV-the first structure of a complete set of components of an ATP-dependent protease. HslV and HslU display sixfold symmetry, ruling out mechanisms of protease activation that require a symmetry mismatch between the two components. Instead, there is conformational flexibility and domain motion in HslU and a localized order-disorder transition in HslV. Individual subunits of HslU contain two globular domains in relative orientations that correlate with nucleotide bound and unbound states. They are surprisingly similar to their counterparts in N-ethylmaleimide-sensitive fusion protein, the prototype of an AAA-ATPase. A third, mostly alpha-helical domain in HslU mediates the contact with HslV and may be the structural equivalent of the amino-terminal domains in proteasomal AAA-ATPases.

==About this Structure==

1DO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ANP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DO2 OCA].

1DO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DO2 OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Bartunik, H.D.]]

[[Category: Bartunik, H D.]]

[[Category: Bochtler, M.]]

[[Category: Bourenkov, G.P.]]

[[Category: Bourenkov, G P.]]

[[Category: Hartmann, C.]]

[[Category: Song, H.K.]]

[[Category: Song, H K.]]

[[Category: ANP]]

[[Category: aaa-atpase]]

Line 25:

[[Category: proteasome]]

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@@ Line 1: / Line 1: @@
-[[Image:1do2.gif|left|200px]]<br /><applet load="1do2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1do2.gif|left|200px]]<br /><applet load="1do2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1do2, resolution 4.00&Aring;" />
 '''TRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI'''<br />
 ==Overview==
-The degradation of cytoplasmic proteins is an ATP-dependent process., Substrates are targeted to a single soluble protease, the 26S proteasome, in eukaryotes and to a number of unrelated proteases in prokaryotes. A, surprising link emerged with the discovery of the ATP-dependent protease, HslVU (heat shock locus VU) in Escherichia coli. Its protease component, HslV shares approximately 20% sequence similarity and a conserved fold, with 20S proteasome beta-subunits. HslU is a member of the Hsp100 (Clp), family of ATPases. Here we report the crystal structures of free HslU and, an 820,000 relative molecular mass complex of HslU and HslV-the first, structure of a complete set of components of an ATP-dependent protease., HslV and HslU display sixfold symmetry, ruling out mechanisms of protease, activation that require a symmetry mismatch between the two components., Instead, there is conformational flexibility and domain motion in HslU and, a localized order-disorder transition in HslV. Individual subunits of HslU, contain two globular domains in relative orientations that correlate with, nucleotide bound and unbound states. They are surprisingly similar to, their counterparts in N-ethylmaleimide-sensitive fusion protein, the, prototype of an AAA-ATPase. A third, mostly alpha-helical domain in HslU, mediates the contact with HslV and may be the structural equivalent of the, amino-terminal domains in proteasomal AAA-ATPases.
+The degradation of cytoplasmic proteins is an ATP-dependent process. Substrates are targeted to a single soluble protease, the 26S proteasome, in eukaryotes and to a number of unrelated proteases in prokaryotes. A surprising link emerged with the discovery of the ATP-dependent protease HslVU (heat shock locus VU) in Escherichia coli. Its protease component HslV shares approximately 20% sequence similarity and a conserved fold with 20S proteasome beta-subunits. HslU is a member of the Hsp100 (Clp) family of ATPases. Here we report the crystal structures of free HslU and an 820,000 relative molecular mass complex of HslU and HslV-the first structure of a complete set of components of an ATP-dependent protease. HslV and HslU display sixfold symmetry, ruling out mechanisms of protease activation that require a symmetry mismatch between the two components. Instead, there is conformational flexibility and domain motion in HslU and a localized order-disorder transition in HslV. Individual subunits of HslU contain two globular domains in relative orientations that correlate with nucleotide bound and unbound states. They are surprisingly similar to their counterparts in N-ethylmaleimide-sensitive fusion protein, the prototype of an AAA-ATPase. A third, mostly alpha-helical domain in HslU mediates the contact with HslV and may be the structural equivalent of the amino-terminal domains in proteasomal AAA-ATPases.
 ==About this Structure==
-DO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ANP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DO2 OCA].
+DO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DO2 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Bartunik, H.D.]]
+[[Category: Bartunik, H D.]]
 [[Category: Bochtler, M.]]
-[[Category: Bourenkov, G.P.]]
+[[Category: Bourenkov, G P.]]
 [[Category: Hartmann, C.]]
-[[Category: Song, H.K.]]
+[[Category: Song, H K.]]
 [[Category: ANP]]
 [[Category: aaa-atpase]]
@@ Line 25: / Line 25: @@
 [[Category: proteasome]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:26:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:36 2008''