1r8j

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(New page: 200px<br /><applet load="1r8j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r8j, resolution 2.03&Aring;" /> '''Crystal Structure of...)
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[[Image:1r8j.jpg|left|200px]]<br /><applet load="1r8j" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of Circadian Clock Protein KaiA from Synechococcus elongatus'''<br />
'''Crystal Structure of Circadian Clock Protein KaiA from Synechococcus elongatus'''<br />
==Overview==
==Overview==
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The circadian clock found in Synechococcus elongatus, the most ancient, circadian clock, is regulated by the interaction of three proteins, KaiA, KaiB, and KaiC. While the precise function of these proteins remains, unclear, KaiA has been shown to be a positive regulator of the expression, of KaiB and KaiC. The 2.0-A structure of KaiA of S. elongatus reported, here shows that the protein is composed of two independently folded, domains connected by a linker. The NH(2)-terminal pseudo-receiver domain, has a similar fold with that of bacterial response regulators, whereas the, COOH-terminal four-helix bundle domain is novel and forms the interface of, the 2-fold-related homodimer. The COOH-terminal four-helix bundle domain, has been shown to contain the KaiC binding site. The structure suggests, that the KaiB binding site is covered in the dimer interface of the KaiA, "closed" conformation, observed in the crystal structure, which suggests, an allosteric regulation mechanism.
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The circadian clock found in Synechococcus elongatus, the most ancient circadian clock, is regulated by the interaction of three proteins, KaiA, KaiB, and KaiC. While the precise function of these proteins remains unclear, KaiA has been shown to be a positive regulator of the expression of KaiB and KaiC. The 2.0-A structure of KaiA of S. elongatus reported here shows that the protein is composed of two independently folded domains connected by a linker. The NH(2)-terminal pseudo-receiver domain has a similar fold with that of bacterial response regulators, whereas the COOH-terminal four-helix bundle domain is novel and forms the interface of the 2-fold-related homodimer. The COOH-terminal four-helix bundle domain has been shown to contain the KaiC binding site. The structure suggests that the KaiB binding site is covered in the dimer interface of the KaiA "closed" conformation, observed in the crystal structure, which suggests an allosteric regulation mechanism.
==About this Structure==
==About this Structure==
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1R8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R8J OCA].
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1R8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8J OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Synechococcus elongatus]]
[[Category: Synechococcus elongatus]]
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[[Category: LiWang, A.C.]]
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[[Category: LiWang, A C.]]
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[[Category: Sacchettini, J.C.]]
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[[Category: Sacchettini, J C.]]
[[Category: Vakonakis, I.]]
[[Category: Vakonakis, I.]]
[[Category: Ye, S.]]
[[Category: Ye, S.]]
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[[Category: kaia]]
[[Category: kaia]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:21:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:23 2008''

Revision as of 12:48, 21 February 2008


1r8j, resolution 2.03Å

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Crystal Structure of Circadian Clock Protein KaiA from Synechococcus elongatus

Overview

The circadian clock found in Synechococcus elongatus, the most ancient circadian clock, is regulated by the interaction of three proteins, KaiA, KaiB, and KaiC. While the precise function of these proteins remains unclear, KaiA has been shown to be a positive regulator of the expression of KaiB and KaiC. The 2.0-A structure of KaiA of S. elongatus reported here shows that the protein is composed of two independently folded domains connected by a linker. The NH(2)-terminal pseudo-receiver domain has a similar fold with that of bacterial response regulators, whereas the COOH-terminal four-helix bundle domain is novel and forms the interface of the 2-fold-related homodimer. The COOH-terminal four-helix bundle domain has been shown to contain the KaiC binding site. The structure suggests that the KaiB binding site is covered in the dimer interface of the KaiA "closed" conformation, observed in the crystal structure, which suggests an allosteric regulation mechanism.

About this Structure

1R8J is a Single protein structure of sequence from Synechococcus elongatus. Full crystallographic information is available from OCA.

Reference

Crystal structure of circadian clock protein KaiA from Synechococcus elongatus., Ye S, Vakonakis I, Ioerger TR, LiWang AC, Sacchettini JC, J Biol Chem. 2004 May 7;279(19):20511-8. Epub 2004 Mar 8. PMID:15007067

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