2QWS

Neutron and X-ray structural studies of short hydrogen bonds in Photoactive Yellow Protein (PYP)

2QWS の概要

• エントリーDOI: 10.2210/pdb2qws/pdb
• 分子名称: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: neutron, hydrogen bond, photocycle, chromophore, photoreceptor protein, receptor, sensory transduction, signaling protein
• 由来する生物種: Halorhodospira halophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14052.73

構造登録者

Fisher, S.Z.,Langan, P. (登録日: 2007-08-10, 公開日: 2008-03-18, 最終更新日: 2023-08-30)

主引用文献

Fisher, S.Z.,Anderson, S.,Henning, R.,Moffat, K.,Langan, P.,Thiyagarajan, P.,Schultz, A.J.
Neutron and X-ray structural studies of short hydrogen bonds in photoactive yellow protein (PYP)
Acta Crystallogr.,Sect.D, 63:1178-1184, 2007

PubMed Abstract: Photoactive yellow protein (PYP) from Halorhodospira halophila is a soluble 14 kDa blue-light photoreceptor. It absorbs light via its para-coumaric acid chromophore (pCA), which is covalently attached to Cys69 and is believed to be involved in the negative phototactic response of the organism to blue light. The complete structure (including H atoms) of PYP has been determined in D(2)O-soaked crystals through the application of joint X-ray (1.1 A) and neutron (2.5 A) structure refinement in combination with cross-validated maximum-likelihood simulated annealing. The resulting XN structure reveals that the phenolate O atom of pCA accepts deuterons from Glu46 O(epsilon2) and Tyr42 O(eta) in two unusually short hydrogen bonds. This arrangement is stabilized by the donation of a deuteron from Thr50 O(gamma1) to Tyr42 O(eta). However, the deuteron position between pCA and Tyr42 is only partially occupied. Thus, this atom may also interact with Thr50, possibly being disordered or fluctuating between the two bonds.

PubMed: 18007033
DOI: 10.1107/S0907444907047646

実験手法

X-RAY DIFFRACTION (2.5 Å)