4Q3I

Structure of the OsSERK2 leucine rich repeat extracellular domain

4Q3I の概要

• エントリーDOI: 10.2210/pdb4q3i/pdb
• 関連するPDBエントリー: 4Q3G
• 分子名称: OsSERK2 D128N, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: leucine rich repete, toll-like receptor, brassinosteroids, transferase
• 由来する生物種: Oryza sativa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54955.77

構造登録者

McAndrew, R.P.,Pruitt, R.N.,Kamita, S.G.,Pereira, J.H.,Majumder, D.,Hammock, B.D.,Adams, P.D.,Ronald, P.C. (登録日: 2014-04-11, 公開日: 2014-11-12, 最終更新日: 2024-11-06)

主引用文献

McAndrew, R.,Pruitt, R.N.,Kamita, S.G.,Pereira, J.H.,Majumdar, D.,Hammock, B.D.,Adams, P.D.,Ronald, P.C.
Structure of the OsSERK2 leucine-rich repeat extracellular domain.
Acta Crystallogr.,Sect.D, 70:3080-3086, 2014

PubMed Abstract: Somatic embryogenesis receptor kinases (SERKs) are leucine-rich repeat (LRR)-containing integral membrane receptors that are involved in the regulation of development and immune responses in plants. It has recently been shown that rice SERK2 (OsSERK2) is essential for XA21-mediated resistance to the pathogen Xanthomonas oryzae pv. oryzae. OsSERK2 is also required for the BRI1-mediated, FLS2-mediated and EFR-mediated responses to brassinosteroids, flagellin and elongation factor Tu (EF-Tu), respectively. Here, crystal structures of the LRR domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable lymphocyte receptor (VLR) fusions, are reported. These structures suggest that the aspartate mutation does not generate any significant conformational change in the protein, but instead leads to an altered interaction with partner receptors.

PubMed: 25372696
DOI: 10.1107/S1399004714021178

実験手法

X-RAY DIFFRACTION (2.35 Å)