7dxq

Crystal Structure of Cyanobacterial Circadian Clock Protein KaiCCrystal Structure of Cyanobacterial Circadian Clock Protein KaiC

Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Spatiotemporal allostery is the source of complex but ordered biological phenomena. To identify the structural basis for allostery that drives the cyanobacterial circadian clock, we crystallized the clock protein KaiC in four distinct states, which cover a whole cycle of phosphor-transfer events at Ser(431) and Thr(432). The minimal set of allosteric events required for oscillatory nature is a bidirectional coupling between the coil-to-helix transition of the Ser(431)-dependent phospho-switch in the C-terminal domain of KaiC and adenosine 5'-diphosphate release from its N-terminal domain during adenosine triphosphatase cycle. An engineered KaiC protein oscillator consisting of a minimal set of the identified master allosteric events exhibited a monophosphorylation cycle of Ser(431) with a temperature-compensated circadian period, providing design principles for simple posttranslational biochemical circadian oscillators. Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.,Furuike Y, Mukaiyama A, Ouyang D, Ito-Miwa K, Simon D, Yamashita E, Kondo T, Akiyama S Sci Adv. 2022 Apr 15;8(15):eabm8990. doi: 10.1126/sciadv.abm8990. Epub 2022 Apr, 15. PMID:35427168 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Circadian clock protein 3D structures

spinqualitylabelsall models 7dxq, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image