4TLB: Crystal Structure Of N-terminal C1 Domain Of Kaic

Citation:
Abstract
Circadian clocks generate slow and ordered cellular dynamics but consist of fast-moving bio-macromolecules; consequently, the origins of the overall slowness remain unclear. We identified the adenosine triphosphate (ATP) catalytic region [adenosine triphosphatase (ATPase)] in the amino-terminal half of the clock protein KaiC as the minimal pacemaker that controls the in vivo frequency of the cyanobacterial clock. Crystal structures of the ATPase revealed that the slowness of this ATPase arises from sequestration of a lytic water molecule in an unfavorable position and coupling of ATP hydrolysis to a peptide isomerization with high activation energy. The slow ATPase is coupled with another ATPase catalyzing autodephosphorylation in the carboxyl-terminal half of KaiC, yielding the circadian response frequency of intermolecular interactions with other clock-related proteins that influences the transcription and translation cycle.
PDB ID: 4TLBDownload
MMDB ID: 130486
PDB Deposition Date: 2014/5/29
Updated in MMDB: 2015/08
Experimental Method:
x-ray diffraction
Resolution: 1.98  Å
Source Organism:
Similar Structures:
Biological Unit for 4TLB: hexameric; determined by author and by software (PISA)
Molecular Components in 4TLB
Label Count Molecule
Proteins (6 molecules)
6
Circadian Clock Protein Kinase Kaic
Molecule annotation
Chemicals (18 molecules)
1
6
2
6
3
6
* Click molecule labels to explore molecular sequence information.

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