1M2F
Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Family of 25 structures
Summary for 1M2F
| Entry DOI | 10.2210/pdb1m2f/pdb |
| Related | 1m2e |
| NMR Information | BMRB: 5031 |
| Descriptor | KaiA (1 entity in total) |
| Functional Keywords | alpha-beta-alpha sandwich, circadian clock protein |
| Biological source | Synechococcus elongatus |
| Total number of polymer chains | 1 |
| Total formula weight | 15077.12 |
| Authors | Williams, S.B.,Vakonakis, I.,Golden, S.S.,LiWang, A.C. (deposition date: 2002-06-23, release date: 2002-11-13, Last modification date: 2024-05-22) |
| Primary citation | Williams, S.B.,Vakonakis, I.,Golden, S.S.,LiWang, A.C. Structure and Function from the Circadian Clock Protein KaiA of Synechococcus elongatus: A potential Clock Input Mechanism Proc.Natl.Acad.Sci.USA, 99:15357-15362, 2002 Cited by PubMed Abstract: In the cyanobacterium Synechococcus elongatus (PCC 7942) the proteins KaiA, KaiB, and KaiC are required for circadian clock function. We deduced a circadian clock function for KaiA from a combination of biochemical and structural data. Both KaiA and its isolated carboxyl-terminal domain (KaiA180C) stimulated KaiC autophosphorylation and facilitated attenuation of KaiC autophosphorylation by KaiB. An amino-terminal domain (KaiA135N) had no function in the autophosphorylation assay. NMR structure determination showed that KaiA135N is a pseudo-receiver domain. We propose that this pseudo-receiver is a timing input-device that regulates KaiA stimulation of KaiC autophosphorylation, which in turn is essential for circadian timekeeping. PubMed: 12438647DOI: 10.1073/pnas.232517099 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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