7XBR

Crystal structure of phosphorylated AtMKK5

Summary for 7XBR

• Entry DOI: 10.2210/pdb7xbr/pdb
• Descriptor: Mitogen-activated protein kinase kinase 5 (2 entities in total)
• Functional Keywords: mitogen-activated protein kinase kinase 5, arabidopsis thaliana, phosphoserine, phosphothreonine, transferase
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 8
• Total formula weight: 266979.26

Authors

Pei, C.J.,Luo, Z.P.,Wu, J.W.,Wang, Z.X. (deposition date: 2022-03-22, release date: 2023-02-08, Last modification date: 2024-10-16)

Primary citation

Pei, C.J.,He, Q.X.,Luo, Z.,Yao, H.,Wang, Z.X.,Wu, J.W.
Crystal structure of the phosphorylated Arabidopsis MKK5 reveals activation mechanism of MAPK kinases.
Acta Biochim.Biophys.Sin., 54:1159-1170, 2022

PubMed Abstract: The mitogen-activated protein kinase (MAPK) signaling pathways are highly conserved in eukaryotes, regulating various cellular processes. The MAPK kinases (MKKs) are dual specificity kinases, serving as convergence and divergence points of the tripartite MAPK cascades. Here, we investigate the biochemical characteristics and three-dimensional structure of MKK5 in (AtMKK5). The recombinant full-length AtMKK5 is phosphorylated and can activate its physiological substrate AtMPK6. There is a conserved kinase interacting motif (KIM) at the N-terminus of AtMKK5, indispensable for specific recognition of AtMPK6. The kinase domain of AtMKK5 adopts active conformation, of which the extended activation segment is stabilized by the phosphorylated Ser221 and Thr215 residues. In line with sequence divergence from other MKKs, the αD and αK helices are missing in AtMKK5, suggesting that the AtMKK5 may adopt distinct modes of upstream kinase/substrate binding. Our data shed lights on the molecular mechanisms of MKK activation and substrate recognition, which may help design specific inhibitors targeting human and plant MKKs.

PubMed: 35866601
DOI: 10.3724/abbs.2022089

Experimental method

X-RAY DIFFRACTION (3.2 Å)