1jon: Difference between revisions

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

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

caption="1jon, resolution 2.5Å" />

'''GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345'''<br />

==Overview==

The chaperonin GroEL is a large complex composed of 14 identical 57-kDa, subunits that requires ATP and GroES for some of its activities. We find, that a monomeric polypeptide corresponding to residues 191 to 345 has the, activity of the tetradecamer both in facilitating the refolding of, rhodanese and cyclophilin A in the absence of ATP and in catalyzing the, unfolding of native barnase. Its crystal structure, solved at 2.5 A, resolution, shows a well-ordered domain with the same fold as in intact, GroEL. We have thus isolated the active site of the complex allosteric, molecular chaperone, which functions as a "minichaperone." This has, mechanistic implications: the presence of a central cavity in the GroEL, complex is not essential for those representative activities in vitro, and, neither are the allosteric properties. The function of the allosteric, behavior on the binding of GroES and ATP must be to regulate the affinity, of the protein for its various substrates in vivo, where the cavity may, also be required for special functions.

The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and cyclophilin A in the absence of ATP and in catalyzing the unfolding of native barnase. Its crystal structure, solved at 2.5 A resolution, shows a well-ordered domain with the same fold as in intact GroEL. We have thus isolated the active site of the complex allosteric molecular chaperone, which functions as a "minichaperone." This has mechanistic implications: the presence of a central cavity in the GroEL complex is not essential for those representative activities in vitro, and neither are the allosteric properties. The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions.

==About this Structure==

1JON 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=1JON OCA].

1JON 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=1JON OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Buckle, A.M.]]

[[Category: Buckle, A M.]]

[[Category: Fersht, A.R.]]

[[Category: Fersht, A R.]]

[[Category: atp-binding]]

[[Category: cell division]]

Line 20:

[[Category: phosphorylation]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:00 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1jon.jpg|left|200px]]<br /><applet load="1jon" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jon.jpg|left|200px]]<br /><applet load="1jon" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jon, resolution 2.5&Aring;" />
 '''GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345'''<br />
 ==Overview==
-The chaperonin GroEL is a large complex composed of 14 identical 57-kDa, subunits that requires ATP and GroES for some of its activities. We find, that a monomeric polypeptide corresponding to residues 191 to 345 has the, activity of the tetradecamer both in facilitating the refolding of, rhodanese and cyclophilin A in the absence of ATP and in catalyzing the, unfolding of native barnase. Its crystal structure, solved at 2.5 A, resolution, shows a well-ordered domain with the same fold as in intact, GroEL. We have thus isolated the active site of the complex allosteric, molecular chaperone, which functions as a "minichaperone." This has, mechanistic implications: the presence of a central cavity in the GroEL, complex is not essential for those representative activities in vitro, and, neither are the allosteric properties. The function of the allosteric, behavior on the binding of GroES and ATP must be to regulate the affinity, of the protein for its various substrates in vivo, where the cavity may, also be required for special functions.
+The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and cyclophilin A in the absence of ATP and in catalyzing the unfolding of native barnase. Its crystal structure, solved at 2.5 A resolution, shows a well-ordered domain with the same fold as in intact GroEL. We have thus isolated the active site of the complex allosteric molecular chaperone, which functions as a "minichaperone." This has mechanistic implications: the presence of a central cavity in the GroEL complex is not essential for those representative activities in vitro, and neither are the allosteric properties. The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions.
 ==About this Structure==
-JON 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=1JON OCA].
+JON 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=1JON OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Buckle, A.M.]]
+[[Category: Buckle, A M.]]
-[[Category: Fersht, A.R.]]
+[[Category: Fersht, A R.]]
 [[Category: atp-binding]]
 [[Category: cell division]]
@@ Line 20: / Line 20: @@
 [[Category: phosphorylation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:25:53 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:00 2008''