1t4y

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[[Image:1t4y.jpg|left|200px]]
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{{Structure
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|GENE= SASA, SARS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32046 Synechococcus elongatus])
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{{STRUCTURE_1t4y| PDB=1t4y | SCENE= }}
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|RELATEDENTRY=[[1t4z|1T4Z]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4y OCA], [http://www.ebi.ac.uk/pdbsum/1t4y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t4y RCSB]</span>
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'''Solution structure of the N-terminal domain of Synechococcus elongatus SasA (average minimized structure)'''
'''Solution structure of the N-terminal domain of Synechococcus elongatus SasA (average minimized structure)'''
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[[Category: LiWang, A C.]]
[[Category: LiWang, A C.]]
[[Category: Vakonakis, I.]]
[[Category: Vakonakis, I.]]
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[[Category: alpha/beta protein]]
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[[Category: Alpha/beta protein]]
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[[Category: thioredoxin fold]]
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[[Category: Thioredoxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:32:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:51:22 2008''
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Revision as of 06:32, 3 May 2008

Template:STRUCTURE 1t4y

Solution structure of the N-terminal domain of Synechococcus elongatus SasA (average minimized structure)


Overview

Circadian oscillators are endogenous biological systems that generate the approximately 24 hour temporal pattern of biological processes and confer a reproductive fitness advantage to their hosts. The cyanobacterial clock is the simplest known and the only clock system for which structural information for core component proteins, in this case KaiA, KaiB and KaiC, is available. SasA, a clock-associated histidine kinase, is necessary for robustness of the circadian rhythm of gene expression and implicated in clock output. The N-terminal domain of SasA (N-SasA) interacts directly with KaiC and likely functions as the sensory domain controlling the SasA histidine kinase activity. N-SasA and KaiB share significant sequence similarity and, thus, it has been proposed that they would be structurally similar and may even compete for KaiC binding. Here, we report the NMR structure of N-SasA and show it to be different from that of KaiB. The structural comparisons provide no clear details to suggest competition of SasA and KaiB for KaiC binding. N-SasA adopts a canonical thioredoxin fold but lacks the catalytic cysteine residues. A patch of conserved, solvent-exposed residues is found near the canonical thioredoxin active site. We suggest that this surface is used by N-SasA for protein-protein interactions. Our analysis suggests that the structural differences between N-SasA and KaiB are the result of only a few critical amino acid substitutions.

About this Structure

1T4Y is a Single protein structure of sequence from Synechococcus elongatus. Full crystallographic information is available from OCA.

Reference

Structure of the N-terminal domain of the circadian clock-associated histidine kinase SasA., Vakonakis I, Klewer DA, Williams SB, Golden SS, LiWang AC, J Mol Biol. 2004 Sep 3;342(1):9-17. PMID:15313603 Page seeded by OCA on Sat May 3 09:32:02 2008

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