4TLA

Crystal structure of N-terminal C1 domain of KaiC

Summary for 4TLA

• Entry DOI: 10.2210/pdb4tla/pdb
• Related: 4TL6 4TL7 4TL8 4TL9 4TLB 4TLC 4TLD 4TLE
• Descriptor: Circadian clock protein kinase KaiC, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: serine/threonine-protein kinase, transferase
• Biological source: Synechococcus elongatus PCC 7942
• Total number of polymer chains: 6
• Total formula weight: 173439.14

Authors

Abe, J.,Hiyama, T.B.,Mukaiyama, A.,Son, S.,Akiyama, S. (deposition date: 2014-05-29, release date: 2015-07-01, Last modification date: 2024-03-20)

Primary citation

Abe, J.,Hiyama, T.B.,Mukaiyama, A.,Son, S.,Mori, T.,Saito, S.,Osako, M.,Wolanin, J.,Yamashita, E.,Kondo, T.,Akiyama, S.
Circadian rhythms. Atomic-scale origins of slowness in the cyanobacterial circadian clock.
Science, 349:312-316, 2015

PubMed 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.

PubMed: 26113637
DOI: 10.1126/science.1261040

Experimental method

X-RAY DIFFRACTION (1.8 Å)