1q6a: Difference between revisions
New page: left|200px<br /><applet load="1q6a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q6a" /> '''Solution Structure of the C-terminal Domain ... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1q6a.jpg|left|200px]]<br /><applet load="1q6a" size=" | [[Image:1q6a.jpg|left|200px]]<br /><applet load="1q6a" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1q6a" /> | caption="1q6a" /> | ||
'''Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Averaged Minimized Structure'''<br /> | '''Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Averaged Minimized Structure'''<br /> | ||
==Overview== | ==Overview== | ||
KaiA is a two-domain circadian clock protein in cyanobacteria, acting as | KaiA is a two-domain circadian clock protein in cyanobacteria, acting as the positive element in a feedback loop that sustains the oscillation. The structure of the N-terminal domain of KaiA is that of a pseudo-receiver, similar to those of bacterial response regulators, which likely interacts with components of the clock-resetting pathway. The C-terminal domain of KaiA is highly conserved among cyanobacteria and enhances the autokinase activity of KaiC. Here we present the NMR structure of the C-terminal domain of KaiA from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. This domain adopts a novel all alpha-helical homodimeric structure. Several mutations known to affect the period of the circadian oscillator are shown to be located at an exposed groove near the dimer interface. This NMR structure and a 21-A-resolution electron microscopy structure of the hexameric KaiC particle allow us to postulate a mode of KaiA-KaiC interaction, in which KaiA binds a linker region connecting two globular KaiC domains. | ||
==About this Structure== | ==About this Structure== | ||
1Q6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http:// | 1Q6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q6A OCA]. | ||
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Bacteria]] | [[Category: Bacteria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Golden, S | [[Category: Golden, S S.]] | ||
[[Category: Holzenburg, A.]] | [[Category: Holzenburg, A.]] | ||
[[Category: LiWang, A | [[Category: LiWang, A C.]] | ||
[[Category: Sun, J.]] | [[Category: Sun, J.]] | ||
[[Category: Vakonakis, I.]] | [[Category: Vakonakis, I.]] | ||
| Line 21: | Line 21: | ||
[[Category: homodimer]] | [[Category: homodimer]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:19 2008'' | ||
Revision as of 15:36, 21 February 2008
|
Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Averaged Minimized Structure
OverviewOverview
KaiA is a two-domain circadian clock protein in cyanobacteria, acting as the positive element in a feedback loop that sustains the oscillation. The structure of the N-terminal domain of KaiA is that of a pseudo-receiver, similar to those of bacterial response regulators, which likely interacts with components of the clock-resetting pathway. The C-terminal domain of KaiA is highly conserved among cyanobacteria and enhances the autokinase activity of KaiC. Here we present the NMR structure of the C-terminal domain of KaiA from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. This domain adopts a novel all alpha-helical homodimeric structure. Several mutations known to affect the period of the circadian oscillator are shown to be located at an exposed groove near the dimer interface. This NMR structure and a 21-A-resolution electron microscopy structure of the hexameric KaiC particle allow us to postulate a mode of KaiA-KaiC interaction, in which KaiA binds a linker region connecting two globular KaiC domains.
About this StructureAbout this Structure
1Q6A is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interaction., Vakonakis I, Sun J, Wu T, Holzenburg A, Golden SS, LiWang AC, Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1479-84. Epub 2004 Jan 28. PMID:14749515
Page seeded by OCA on Thu Feb 21 14:36:19 2008