1dky: Difference between revisions

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

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

caption="1dky, resolution 2.8Å" />

'''THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 2 NATIVE CRYSTALS'''<br />

==Overview==

DnaK and other members of the 70-kilodalton heat-shock protein (hsp70), family promote protein folding, interaction, and translocation, both, constitutively and in response to stress, by binding to unfolded, polypeptide segments. These proteins have two functional units: a, substrate-binding portion binds the polypeptide, and an adenosine, triphosphatase portion facilitates substrate exchange. The crystal, structure of a peptide complex with the substrate-binding unit of DnaK has, now been determined at 2.0 angstroms resolution. The structure consists of, a beta-sandwich subdomain followed by alpha-helical segments. The peptide, is bound to DnaK in an extended conformation through a channel defined by, loops from the beta sandwich. An alpha-helical domain stabilizes the, complex, but does not contact the peptide directly. This domain is rotated, in the molecules of a second crystal lattice, which suggests a model of, conformation-dependent substrate binding that features a latch mechanism, for maintaining long lifetime complexes.

DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 angstroms resolution. The structure consists of a beta-sandwich subdomain followed by alpha-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the beta sandwich. An alpha-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.

==About this Structure==

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

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

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Burkholder, W.F.]]

[[Category: Burkholder, W F.]]

[[Category: Gottesman, M.E.]]

[[Category: Gottesman, M E.]]

[[Category: Gragerov, A.]]

[[Category: Hendrickson, W.A.]]

[[Category: Hendrickson, W A.]]

[[Category: Ogata, C.M.]]

[[Category: Ogata, C M.]]

[[Category: Zhao, X.]]

[[Category: Zhu, X.]]

Line 24:

[[Category: heat shock protein 70 kda (hsp70)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:22:~~37 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:39 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dky.gif|left|200px]]<br /><applet load="1dky" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dky.gif|left|200px]]<br /><applet load="1dky" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dky, resolution 2.8&Aring;" />
 '''THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 2 NATIVE CRYSTALS'''<br />
 ==Overview==
-DnaK and other members of the 70-kilodalton heat-shock protein (hsp70), family promote protein folding, interaction, and translocation, both, constitutively and in response to stress, by binding to unfolded, polypeptide segments. These proteins have two functional units: a, substrate-binding portion binds the polypeptide, and an adenosine, triphosphatase portion facilitates substrate exchange. The crystal, structure of a peptide complex with the substrate-binding unit of DnaK has, now been determined at 2.0 angstroms resolution. The structure consists of, a beta-sandwich subdomain followed by alpha-helical segments. The peptide, is bound to DnaK in an extended conformation through a channel defined by, loops from the beta sandwich. An alpha-helical domain stabilizes the, complex, but does not contact the peptide directly. This domain is rotated, in the molecules of a second crystal lattice, which suggests a model of, conformation-dependent substrate binding that features a latch mechanism, for maintaining long lifetime complexes.
+DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 angstroms resolution. The structure consists of a beta-sandwich subdomain followed by alpha-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the beta sandwich. An alpha-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.
 ==About this Structure==
-DKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DKY OCA].
+DKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKY OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Burkholder, W.F.]]
+[[Category: Burkholder, W F.]]
-[[Category: Gottesman, M.E.]]
+[[Category: Gottesman, M E.]]
 [[Category: Gragerov, A.]]
-[[Category: Hendrickson, W.A.]]
+[[Category: Hendrickson, W A.]]
-[[Category: Ogata, C.M.]]
+[[Category: Ogata, C M.]]
 [[Category: Zhao, X.]]
 [[Category: Zhu, X.]]
@@ Line 24: / Line 24: @@
 [[Category: heat shock protein 70 kda (hsp70)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:22:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:39 2008''