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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Neutron and X-ray structural studies of short hydrogen bonds in photoactive yellow protein (PYP).
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Neutron and X-ray structural studies of short hydrogen bonds in photoactive yellow protein (PYP).

机译：中子和x射线结构研究短氢键在黄色光活化的蛋白质

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摘要

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.
机译：黄色光活化的蛋白(PYP)Halorhodospira halophila可溶性14 kDa探讨蓝光光感受器。其para-coumaric酸发色团(pCA)是Cys69共价结合,相信吗参与消极phototactic反应的生物蓝光。PYP的完整结构(包括H原子)在D(2)确定O-soaked晶体联合应用x射线(1.1)中子结构细化(2.5)结合旨在最大似然模拟退火。结果XN结构表明,酚盐O原子Glu46 pCA接受氘核的O (epsilon2)和Tyr42 O (eta)在两个不同寻常的短的氢键。稳定的氘核的捐赠Thr50 O(γ)Tyr42 O (eta)。氘核位置pCA和Tyr42之间部分占领。与Thr50交互,可能被无序或两个键之间的波动。

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