7P8E
Crystal structure of the Receiver domain of M. truncatula cytokinin receptor MtCRE1
Summary for 7P8E
| Entry DOI | 10.2210/pdb7p8e/pdb |
| Descriptor | Receiver domain of histidine kinase, CALCIUM ION (3 entities in total) |
| Functional Keywords | flavodoxin-like fold, cytokinin, phosphorelay, signaling protein |
| Biological source | Medicago truncatula (Barrel medic, Medicago tribuloides) |
| Total number of polymer chains | 1 |
| Total formula weight | 71366.50 |
| Authors | Tran, L.H.,Urbanowicz, A.,Jasinski, M.,Jaskolski, M.,Ruszkowski, M. (deposition date: 2021-07-21, release date: 2021-10-20, Last modification date: 2024-01-31) |
| Primary citation | Tran, L.H.,Urbanowicz, A.,Jasinski, M.,Jaskolski, M.,Ruszkowski, M. 3D Domain Swapping Dimerization of the Receiver Domain of Cytokinin Receptor CRE1 From Arabidopsis thaliana and Medicago truncatula . Front Plant Sci, 12:756341-756341, 2021 Cited by PubMed Abstract: Cytokinins are phytohormones regulating many biological processes that are vital to plants. CYTOKININ RESPONSE1 (CRE1), the main cytokinin receptor, has a modular architecture composed of a cytokinin-binding CHASE (Cyclases/Histidine kinases Associated Sensory Extracellular) domain, followed by a transmembrane fragment, an intracellular histidine kinase (HK) domain, and a receiver domain (REC). Perception of cytokinin signaling involves (i) a hormone molecule binding to the CHASE domain, (ii) CRE1 autophosphorylation at a conserved His residue in the HK domain, followed by a phosphorelay to (iii) a conserved Asp residue in the REC domain, (iv) a histidine-containing phosphotransfer protein (HPt), and (v) a response regulator (RR). This work focuses on the crystal structures of the REC domain of CRE1 from the model plant and from the model legume . Both REC domains form tight 3D-domain-swapped dimers. Dimerization of the REC domain agrees with the quaternary assembly of the entire CRE1 but is incompatible with a model of its complex with HPt, suggesting that a considerable conformational change should occur to enable the signal transduction. Indeed, phosphorylation of the REC domain can change the HPt-binding properties of CRE1, as shown by functional studies. PubMed: 34630499DOI: 10.3389/fpls.2021.756341 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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