2QWS

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

Summary for 2QWS

• Entry DOI: 10.2210/pdb2qws/pdb
• Descriptor: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• Functional Keywords: neutron, hydrogen bond, photocycle, chromophore, photoreceptor protein, receptor, sensory transduction, signaling protein
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 14052.73

Authors

Fisher, S.Z.,Langan, P. (deposition date: 2007-08-10, release date: 2008-03-18, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)