4HHD

2.75 Angstrom resolution crystal structure of the A. thaliana LOV2 domain with an extended N-terminal A' helix (cryo dark structure)

4HHD の概要

• エントリーDOI: 10.2210/pdb4hhd/pdb
• 分子名称: Phototropin-1, FLAVIN MONONUCLEOTIDE, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: lov2, kinase, transferase, atp-binding, arabidopsis thaliana, serine/threonine-protein kinase, light-induced signal transduction, phototropin-1, lov (pas) domain
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Cell membrane; Peripheral membrane protein: O48963
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39175.01

構造登録者

Halavaty, A.S.,Moffat, K. (登録日: 2012-10-09, 公開日: 2013-10-09, 最終更新日: 2023-09-20)

主引用文献

Halavaty, A.S.,Moffat, K.
Coiled-coil dimerization of the LOV2 domain of the blue-light photoreceptor phototropin 1 from Arabidopsis thaliana.
Acta Crystallogr.,Sect.F, 69:1316-1321, 2013

PubMed Abstract: A key role in signal transduction and dimerization mediated by Per-Arnt-Sim (PAS) domains is played by α-helical linkers that flank the structurally similar α/β cores of these domains. However, crystal-packing forces and the different construct lengths and sequences of the PAS domains influence the final length and orientation of the linkers relative to the core and create uncertainty in the exact mechanism of the linker function. Thus, structural characterization and comparison of the linkers within isolated PAS-domain constructs and/or full-length PAS-containing proteins is important for clarification of the mechanism. The plant blue-light photoreceptors phototropins possess two N-terminal flavin mononucleotide-based light, oxygen or voltage (LOV) domains (LOV1 and LOV2) that comprise a subclass of the PAS family and one C-terminal serine/threonine kinase domain whose enzymatic activity is regulated by blue light. The dark-adapted state crystal structures of the Arabidopsis thaliana phototropin 1 and phototropin 2 LOV1-domain constructs flanked by an N-terminal A'α helix and the structure of the phototropin 2 core LOV2 domain are known. Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state. The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix similar to those in the previously reported structure of Avena sativa phototropin 1 LOV2. In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer in which two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil. The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.

PubMed: 24316821
DOI: 10.1107/S1744309113029199

実験手法

X-RAY DIFFRACTION (2.75 Å)