5LPB

Crystal structure of the BRI1 kinase domain (865-1160) in complex with ADP from Arabidopsis thaliana

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5LPB の概要

• エントリーDOI: 10.2210/pdb5lpb/pdb
• 分子名称: Protein BRASSINOSTEROID INSENSITIVE 1, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: brassinosteroid receptor, kinase domain, dual-specificify kinase, membrane receptor kinase, plasma membrane, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: O22476
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33869.40

構造登録者

Bojar, D.,Martinez, J.,Hothorn, M. (登録日: 2016-08-12, 公開日: 2016-08-31, 最終更新日: 2024-10-09)

主引用文献

Bojar, D.,Martinez, J.,Santiago, J.,Rybin, V.,Bayliss, R.,Hothorn, M.
Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation.
Plant J., 78:31-43, 2014

PubMed Abstract: Brassinosteroids, which control plant growth and development, are sensed by the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1). Brassinosteroid binding to the BRI1 leucine-rich repeat (LRR) domain induces heteromerisation with a SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK)-family co-receptor. This process allows the cytoplasmic kinase domains of BRI1 and SERK to interact, trans-phosphorylate and activate each other. Here we report crystal structures of the BRI1 kinase domain in its activated form and in complex with nucleotides. BRI1 has structural features reminiscent of both serine/threonine and tyrosine kinases, providing insight into the evolution of dual-specificity kinases in plants. Phosphorylation of Thr1039, Ser1042 and Ser1044 causes formation of a catalytically competent activation loop. Mapping previously identified serine/threonine and tyrosine phosphorylation sites onto the structure, we analyse their contribution to brassinosteroid signaling. The location of known genetic missense alleles provide detailed insight into the BRI1 kinase mechanism, while our analyses are inconsistent with a previously reported guanylate cyclase activity. We identify a protein interaction surface on the C-terminal lobe of the kinase and demonstrate that the isolated BRI1, SERK2 and SERK3 cytoplasmic segments form homodimers in solution and have a weak tendency to heteromerise. We propose a model in which heterodimerisation of the BRI1 and SERK ectodomains brings their cytoplasmic kinase domains in a catalytically competent arrangement, an interaction that can be modulated by the BRI1 inhibitor protein BKI1.

PubMed: 24461462
DOI: 10.1111/tpj.12445

実験手法

X-RAY DIFFRACTION (1.98 Å)