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Crystallization and preliminary X‐ray crystallographic study of human Hikeshi, a new nuclear transport receptor for Hsp70
Author(s) -
Song Jinsue,
Lee Soo Jae
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14024145
Subject(s) - importin , crystallization , mutant , crystallography , nuclear transport , hsp70 , heat shock protein , hsp90 , receptor , chemistry , biochemistry , cell nucleus , cytoplasm , gene , organic chemistry
Hikeshi is a new nuclear transport receptor that plays an important role in the nuclear import of Hsp70 heat‐shock proteins under thermal stress. Wild‐type human Hikeshi and its Phe97Ala mutant were overproduced and purified using an Escherichia coli expression system. The purified proteins were crystallized using the hanging‐drop vapour‐diffusion technique. Wild‐type crystals grew in space group C 222 1 , with unit‐cell parameters a = 61.1, b = 137.8, c = 97.9 Å, α = 90.0, β = 90.0, γ = 90.0°. Phe97Ala mutant crystals were obtained in space group P 3 2 , with unit‐cell parameters a = 85.7, b = 85.7, c = 69.1 Å, α = 90.0, β = 90.0, γ = 120.0°. These crystals diffracted to 1.8 and 2.5 Å resolution, respectively. This study is the first to yield structural insight into this highly unusual fourth import receptor after importins, NTF2 and TAP.