8EIZ

Cryo-EM structure of squid sensory receptor CRB1

これはPDB形式変換不可エントリーです。

8EIZ の概要

• エントリーDOI: 10.2210/pdb8eiz/pdb
• EMDBエントリー: 28167
• 分子名称: Squid sensory receptor CRB1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, N-benzyl-2-(2,6-dimethylanilino)-N,N-diethyl-2-oxoethan-1-aminium, ... (4 entities in total)
• 機能のキーワード: pentameric ligand gated ion channel, squid sensory receptor, cys-loop receptor, structural protein
• 由来する生物種: Sepioloidea lineolata
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 229753.66

構造登録者

Kang, G.,Kim, J.J.,Allard, C.A.H.,Valencia-Montoya, W.A.,van Giesen, L.,Kilian, P.B.,Bai, X.,Bellono, N.W.,Hibbs, R.E. (登録日: 2022-09-15, 公開日: 2023-04-12, 最終更新日: 2024-10-23)

主引用文献

Kang, G.,Allard, C.A.H.,Valencia-Montoya, W.A.,van Giesen, L.,Kim, J.J.,Kilian, P.B.,Bai, X.,Bellono, N.W.,Hibbs, R.E.
Sensory specializations drive octopus and squid behaviour.
Nature, 616:378-383, 2023

PubMed Abstract: The evolution of new traits enables expansion into new ecological and behavioural niches. Nonetheless, demonstrated connections between divergence in protein structure, function and lineage-specific behaviours remain rare. Here we show that both octopus and squid use cephalopod-specific chemotactile receptors (CRs) to sense their respective marine environments, but structural adaptations in these receptors support the sensation of specific molecules suited to distinct physiological roles. We find that squid express ancient CRs that more closely resemble related nicotinic acetylcholine receptors, whereas octopuses exhibit a more recent expansion in CRs consistent with their elaborated 'taste by touch' sensory system. Using a combination of genetic profiling, physiology and behavioural analyses, we identify the founding member of squid CRs that detects soluble bitter molecules that are relevant in ambush predation. We present the cryo-electron microscopy structure of a squid CR and compare this with octopus CRs and nicotinic receptors. These analyses demonstrate an evolutionary transition from an ancestral aromatic 'cage' that coordinates soluble neurotransmitters or tastants to a more recent octopus CR hydrophobic binding pocket that traps insoluble molecules to mediate contact-dependent chemosensation. Thus, our study provides a foundation for understanding how adaptation of protein structure drives the diversification of organismal traits and behaviour.

PubMed: 37045917
DOI: 10.1038/s41586-023-05808-z

実験手法

ELECTRON MICROSCOPY (3.13 Å)