1k6k: Difference between revisions

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[[Image:1k6k.jpg|left|200px]]<br /><applet load="1k6k" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1k6k.jpg|left|200px]]<br /><applet load="1k6k" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1k6k, resolution 1.8Å" />

'''Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains'''<br />

==Overview==

Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component, of the ATP-dependent ClpAP protease, participates in regulatory protein, degradation and the dissolution and degradation of protein aggregates. The, crystal structure of the ClpA subunit reveals an N-terminal domain with, pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting, of a large and a small sub-domain with ADP bound in the sub-domain, junction. The N-terminal domain interacts with the D1 domain in a manner, similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are, connected head-to-tail consistent with a cooperative and vectorial, translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known, structures of AAA(+) modules, the differences in D1-D1 and D2-D2, interfaces correlate with their respective contributions to hexamer, stability and ATPase activity.

Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity.

==About this Structure==

1K6K 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=1K6K OCA].

1K6K 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=1K6K OCA].

==Reference==

Line 15:

[[Category: Esser, L.]]

[[Category: Guo, F.]]

[[Category: Maurizi, M.R.]]

[[Category: Maurizi, M R.]]

[[Category: Xia, D.]]

[[Category: adaptor binding]]

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[[Category: x-ray]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:41 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1k6k.jpg|left|200px]]<br /><applet load="1k6k" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k6k.jpg|left|200px]]<br /><applet load="1k6k" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k6k, resolution 1.8&Aring;" />
 '''Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains'''<br />
 ==Overview==
-Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component, of the ATP-dependent ClpAP protease, participates in regulatory protein, degradation and the dissolution and degradation of protein aggregates. The, crystal structure of the ClpA subunit reveals an N-terminal domain with, pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting, of a large and a small sub-domain with ADP bound in the sub-domain, junction. The N-terminal domain interacts with the D1 domain in a manner, similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are, connected head-to-tail consistent with a cooperative and vectorial, translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known, structures of AAA(+) modules, the differences in D1-D1 and D2-D2, interfaces correlate with their respective contributions to hexamer, stability and ATPase activity.
+Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity.
 ==About this Structure==
-K6K 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=1K6K OCA].
+K6K 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=1K6K OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Esser, L.]]
 [[Category: Guo, F.]]
-[[Category: Maurizi, M.R.]]
+[[Category: Maurizi, M R.]]
 [[Category: Xia, D.]]
 [[Category: adaptor binding]]
@@ Line 25: / Line 25: @@
 [[Category: x-ray]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:53:24 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:41 2008''