2gbl

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(New page: 200px<br /><applet load="2gbl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gbl, resolution 2.8&Aring;" /> '''Crystal Structure of ...)
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caption="2gbl, resolution 2.8&Aring;" />
'''Crystal Structure of Full Length Circadian Clock Protein KaiC with Phosphorylation Sites'''<br />
'''Crystal Structure of Full Length Circadian Clock Protein KaiC with Phosphorylation Sites'''<br />
==Overview==
==Overview==
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The cyanobacterial circadian clock can be reconstituted in vitro by mixing, recombinant KaiA, KaiB and KaiC proteins with ATP, producing KaiC, phosphorylation and dephosphorylation cycles that have a regular rhythm, with a ca. 24-h period and are temperature-compensated. KaiA and KaiB are, modulators of KaiC phosphorylation, whereby KaiB antagonizes KaiA's, action. Here, we present a complete crystallographic model of the, Synechococcus elongatus KaiC hexamer that includes previously unresolved, portions of the C-terminal regions, and a negative-stain electron, microscopy study of S. elongatus and Thermosynechococcus elongatus BP-1, KaiA-KaiC complexes. Site-directed mutagenesis in combination with EM, reveals that KaiA binds exclusively to the CII half of the KaiC hexamer., The EM-based model of the KaiA-KaiC complex reveals protein-protein, interactions at two sites: the known interaction of the flexible, C-terminal KaiC peptide with KaiA, and a second postulated interaction, between the apical region of KaiA and the ATP binding cleft on KaiC. This, model brings KaiA mutation sites that alter clock period or abolish, rhythmicity into contact with KaiC and suggests how KaiA might regulate, KaiC phosphorylation.
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The cyanobacterial circadian clock can be reconstituted in vitro by mixing recombinant KaiA, KaiB and KaiC proteins with ATP, producing KaiC phosphorylation and dephosphorylation cycles that have a regular rhythm with a ca. 24-h period and are temperature-compensated. KaiA and KaiB are modulators of KaiC phosphorylation, whereby KaiB antagonizes KaiA's action. Here, we present a complete crystallographic model of the Synechococcus elongatus KaiC hexamer that includes previously unresolved portions of the C-terminal regions, and a negative-stain electron microscopy study of S. elongatus and Thermosynechococcus elongatus BP-1 KaiA-KaiC complexes. Site-directed mutagenesis in combination with EM reveals that KaiA binds exclusively to the CII half of the KaiC hexamer. The EM-based model of the KaiA-KaiC complex reveals protein-protein interactions at two sites: the known interaction of the flexible C-terminal KaiC peptide with KaiA, and a second postulated interaction between the apical region of KaiA and the ATP binding cleft on KaiC. This model brings KaiA mutation sites that alter clock period or abolish rhythmicity into contact with KaiC and suggests how KaiA might regulate KaiC phosphorylation.
==About this Structure==
==About this Structure==
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2GBL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GBL OCA].
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2GBL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GBL OCA].
==Reference==
==Reference==
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[[Category: Synechococcus sp.]]
[[Category: Synechococcus sp.]]
[[Category: Egli, M.]]
[[Category: Egli, M.]]
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[[Category: Johnson, C.H.]]
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[[Category: Johnson, C H.]]
[[Category: Mori, T.]]
[[Category: Mori, T.]]
[[Category: Pattanayek, R.]]
[[Category: Pattanayek, R.]]
[[Category: Pattanayek, S.]]
[[Category: Pattanayek, S.]]
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[[Category: Stewart, P.L.]]
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[[Category: Stewart, P L.]]
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[[Category: Williams, D.R.]]
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[[Category: Williams, D R.]]
[[Category: Xu, Y.]]
[[Category: Xu, Y.]]
[[Category: ATP]]
[[Category: ATP]]
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[[Category: kaic]]
[[Category: kaic]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:05:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:07 2008''

Revision as of 15:30, 21 February 2008


2gbl, resolution 2.8Å

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Crystal Structure of Full Length Circadian Clock Protein KaiC with Phosphorylation Sites

Overview

The cyanobacterial circadian clock can be reconstituted in vitro by mixing recombinant KaiA, KaiB and KaiC proteins with ATP, producing KaiC phosphorylation and dephosphorylation cycles that have a regular rhythm with a ca. 24-h period and are temperature-compensated. KaiA and KaiB are modulators of KaiC phosphorylation, whereby KaiB antagonizes KaiA's action. Here, we present a complete crystallographic model of the Synechococcus elongatus KaiC hexamer that includes previously unresolved portions of the C-terminal regions, and a negative-stain electron microscopy study of S. elongatus and Thermosynechococcus elongatus BP-1 KaiA-KaiC complexes. Site-directed mutagenesis in combination with EM reveals that KaiA binds exclusively to the CII half of the KaiC hexamer. The EM-based model of the KaiA-KaiC complex reveals protein-protein interactions at two sites: the known interaction of the flexible C-terminal KaiC peptide with KaiA, and a second postulated interaction between the apical region of KaiA and the ATP binding cleft on KaiC. This model brings KaiA mutation sites that alter clock period or abolish rhythmicity into contact with KaiC and suggests how KaiA might regulate KaiC phosphorylation.

About this Structure

2GBL is a Protein complex structure of sequences from Synechococcus sp. with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Analysis of KaiA-KaiC protein interactions in the cyano-bacterial circadian clock using hybrid structural methods., Pattanayek R, Williams DR, Pattanayek S, Xu Y, Mori T, Johnson CH, Stewart PL, Egli M, EMBO J. 2006 May 3;25(9):2017-28. Epub 2006 Apr 20. PMID:16628225

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