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The crystal structure of the E. coli stress protein YciF
Author(s) -
Hindupur Aditya,
Liu Deqian,
Zhao Yonghong,
Bellamy Henry D.,
White Mark A.,
Fox Robert O.
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062307706
Subject(s) - dimer , crystallography , crystal structure , chemistry , helix (gastropod) , protein structure , resolution (logic) , protein folding , monomer , crystal (programming language) , protein crystallization , stereochemistry , crystallization , biochemistry , biology , organic chemistry , ecology , artificial intelligence , snail , computer science , programming language , polymer
YciF is a protein that is up‐regulated when bacteria experience stress conditions, and is highly conserved in a range of bacterial species. YciF has no known structure or biochemical function. To learn more about its potential molecular function and its role in the bacterial stress response, we solved the crystal structure of YciF at 2.0 Å resolution by the multiple wavelength anomalous diffraction (MAD) technique. YciF is a dimer in solution, and forms a homodimer in the crystal asymmetric unit. The two monomers form a dimer with a molecular twofold axis, with a significant burial of solvent‐accessible surface area. The protein is an all‐alpha protein composed of five helices: a four‐helix bundle, and a short additional helix at the dimer interface. The protein is structurally similar to portions of the diiron‐containing proteins, rubrerythrin and the Bacillus anthracis Dlp‐2.

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