1nwz

From Proteopedia

Revision as of 20:30, 20 November 2007

PYP ULTRA-HIGH RESOLUTION STRUCTURE OF A BACTERIAL PHOTORECEPTOR

Overview

Protein photoreceptors use small-molecule cofactors called chromophores to, detect light. Only under the influence of the receptors' active sites do, these chromophores adopt spectral and photochemical properties that suit, the receptors' functional requirements. This protein-induced change in, chromophore properties is called photochemical tuning and is a prime, example for the general--but poorly understood--process of chemical tuning, through which proteins shape the reactivity of their active-site groups., Here we report the 0.82-A resolution X-ray structure of the bacterial, light receptor photoactive yellow protein (PYP). The unusually precise, structure reveals deviations from expected molecular geometries and, anisotropic atomic displacements in the PYP active site. Our analysis of, these deviations points directly to the intramolecular forces and, active-site dynamics that tune the properties of PYP's chromophore to, absorb blue light, suppress fluorescence, and favor the required, light-driven double-bond isomerization.

About this Structure

1NWZ is a Single protein structure of sequence from Halorhodospira halophila with HC4 as ligand. Full crystallographic information is available from OCA.

Reference

Anticipatory active-site motions and chromophore distortion prime photoreceptor PYP for light activation., Getzoff ED, Gutwin KN, Genick UK, Nat Struct Biol. 2003 Aug;10(8):663-8. PMID:12872160

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