2eu1: Difference between revisions

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[[Image:2eu1.gif|left|200px]]<br /><applet load="2eu1" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2eu1.gif|left|200px]]<br /><applet load="2eu1" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2eu1, resolution 3.29Å" />

'''Crystal structure of the chaperonin GroEL-E461K'''<br />

==Overview==

The chaperonin GroEL adopts a double-ring structure with various modes of, allosteric communication. The simultaneous positive intra-ring and, negative inter-ring co-operativities alternate the functionality of the, folding cavities in both protein rings. Negative inter-ring co-operativity, is maintained through different inter-ring interactions, including a salt, bridge involving Glu 461. Replacement of this residue by Lys modifies the, temperature sensitivity of the substrate-folding activity of this protein, most likely as a result of the loss of inter-ring co-operativity. The, crystal structure of the mutant chaperonin GroELE461K has been determined, at 3.3A and compared with other structures: the wild-type GroEL, an, allosteric defective GroEL double mutant and the GroEL-GroES-(ADP)7, complex. The inter-ring region of the mutant exhibits the following, characteristics: (i) no salt-bridge stabilizes the inter-ring interface;, (ii) the mutated residue plays a central role in defining the relative, ring rotation (of about 22 degrees) around the 7-fold axis; (iii) an, increase in the inter-ring distance and solvent accessibility of the, inter-ring interface; and (iv) a 2-fold reduction in the stabilization, energy of the inter-ring interface, due to the modification of inter-ring, interactions. These characteristics explain how the thermal sensitivity of, the protein's fundamental properties permits GroEL to distinguish, physiological (37 degrees C) from stress (42 degrees C) temperatures.

The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. The simultaneous positive intra-ring and negative inter-ring co-operativities alternate the functionality of the folding cavities in both protein rings. Negative inter-ring co-operativity is maintained through different inter-ring interactions, including a salt bridge involving Glu 461. Replacement of this residue by Lys modifies the temperature sensitivity of the substrate-folding activity of this protein, most likely as a result of the loss of inter-ring co-operativity. The crystal structure of the mutant chaperonin GroELE461K has been determined at 3.3A and compared with other structures: the wild-type GroEL, an allosteric defective GroEL double mutant and the GroEL-GroES-(ADP)7 complex. The inter-ring region of the mutant exhibits the following characteristics: (i) no salt-bridge stabilizes the inter-ring interface; (ii) the mutated residue plays a central role in defining the relative ring rotation (of about 22 degrees) around the 7-fold axis; (iii) an increase in the inter-ring distance and solvent accessibility of the inter-ring interface; and (iv) a 2-fold reduction in the stabilization energy of the inter-ring interface, due to the modification of inter-ring interactions. These characteristics explain how the thermal sensitivity of the protein's fundamental properties permits GroEL to distinguish physiological (37 degrees C) from stress (42 degrees C) temperatures.

==About this Structure==

2EU1 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=2EU1 OCA].

2EU1 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=2EU1 OCA].

==Reference==

Line 15:

[[Category: Agirre, J.]]

[[Category: Cabo-Bilbao, A.]]

[[Category: Guerin, D.M.A.]]

[[Category: Guerin, D M.A.]]

[[Category: Mechaly, A.E.]]

[[Category: Mechaly, A E.]]

[[Category: Muga, A.]]

[[Category: Sot, B.]]

Line 25:

[[Category: hsp60]]

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@@ Line 1: / Line 1: @@
-[[Image:2eu1.gif|left|200px]]<br /><applet load="2eu1" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2eu1.gif|left|200px]]<br /><applet load="2eu1" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2eu1, resolution 3.29&Aring;" />
 '''Crystal structure of the chaperonin GroEL-E461K'''<br />
 ==Overview==
-The chaperonin GroEL adopts a double-ring structure with various modes of, allosteric communication. The simultaneous positive intra-ring and, negative inter-ring co-operativities alternate the functionality of the, folding cavities in both protein rings. Negative inter-ring co-operativity, is maintained through different inter-ring interactions, including a salt, bridge involving Glu 461. Replacement of this residue by Lys modifies the, temperature sensitivity of the substrate-folding activity of this protein, most likely as a result of the loss of inter-ring co-operativity. The, crystal structure of the mutant chaperonin GroELE461K has been determined, at 3.3A and compared with other structures: the wild-type GroEL, an, allosteric defective GroEL double mutant and the GroEL-GroES-(ADP)7, complex. The inter-ring region of the mutant exhibits the following, characteristics: (i) no salt-bridge stabilizes the inter-ring interface;, (ii) the mutated residue plays a central role in defining the relative, ring rotation (of about 22 degrees) around the 7-fold axis; (iii) an, increase in the inter-ring distance and solvent accessibility of the, inter-ring interface; and (iv) a 2-fold reduction in the stabilization, energy of the inter-ring interface, due to the modification of inter-ring, interactions. These characteristics explain how the thermal sensitivity of, the protein's fundamental properties permits GroEL to distinguish, physiological (37 degrees C) from stress (42 degrees C) temperatures.
+The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. The simultaneous positive intra-ring and negative inter-ring co-operativities alternate the functionality of the folding cavities in both protein rings. Negative inter-ring co-operativity is maintained through different inter-ring interactions, including a salt bridge involving Glu 461. Replacement of this residue by Lys modifies the temperature sensitivity of the substrate-folding activity of this protein, most likely as a result of the loss of inter-ring co-operativity. The crystal structure of the mutant chaperonin GroELE461K has been determined at 3.3A and compared with other structures: the wild-type GroEL, an allosteric defective GroEL double mutant and the GroEL-GroES-(ADP)7 complex. The inter-ring region of the mutant exhibits the following characteristics: (i) no salt-bridge stabilizes the inter-ring interface; (ii) the mutated residue plays a central role in defining the relative ring rotation (of about 22 degrees) around the 7-fold axis; (iii) an increase in the inter-ring distance and solvent accessibility of the inter-ring interface; and (iv) a 2-fold reduction in the stabilization energy of the inter-ring interface, due to the modification of inter-ring interactions. These characteristics explain how the thermal sensitivity of the protein's fundamental properties permits GroEL to distinguish physiological (37 degrees C) from stress (42 degrees C) temperatures.
 ==About this Structure==
-EU1 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=2EU1 OCA].
+EU1 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=2EU1 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Agirre, J.]]
 [[Category: Cabo-Bilbao, A.]]
-[[Category: Guerin, D.M.A.]]
+[[Category: Guerin, D M.A.]]
-[[Category: Mechaly, A.E.]]
+[[Category: Mechaly, A E.]]
 [[Category: Muga, A.]]
 [[Category: Sot, B.]]
@@ Line 25: / Line 25: @@
 [[Category: hsp60]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:08:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:30 2008''