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Structure and function of chromophores in R-phycoerythrin at 1.9 Å resolution

✍ Scribed by Tao Jiang; Ji-ping Zhang; Dong-cai Liang

Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
260 KB
Volume
34
Category
Article
ISSN
0887-3585

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✦ Synopsis

The crystal structure of R-Phycoerythrin (R-PE) from Polysiphonia urceolata has been refined to a resolution of 1.9 Å, based on the atomic coordinates of R-PE determined at 2.8 Å resolution, through the use of difference Fourier method and steorochemistry parameters restrained refinement with model adjustment according to the electron density map. Crystallographic R-factor of the refined model is 0.195 (Rfree ϭ 0.282) from 8-1.9 Å. High resolution structure of R-PE showed precise interactions between the chromophores and protein residues, which explained the spectrum characteristic and function of chromophores. Four chiral atoms of phycourobilin (PUB) were identified as C(4)-S, C(16)-S, C(21)-S, and C(20)-R. In addition to the coupling distances of 19 Å to 45 Å between the chromophores which were observed and involved in the energy transfer pathway, high resolution structure of R-PE suggested other pathways of energy transfer, such as the ultrashort distance between ␣140a and ␤155 . It has been proposed that aromatic residues in linker proteins not only influence the conformation of chromophore, but may also bridge chromophores to improve the energy transfer efficiency. Proteins 1999; 34:224-231.

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