Structure determination of the C-terminal fragment of yeast Ski7 using twinned crystal data

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Title
Structure determination of the C-terminal fragment of yeast Ski7 using twinned crystal data
Author(s)
Si Hoon Park; Yong-Boo Kuk; Ji-Young Lee; Byeong-Cheon Jeong; Hyun Kyu Song
Publication Date
2017-03
Journal
Biodesign, v.5, no.1, pp.12 - 23
Publisher
Biodesign
Abstract
The structure determination using twinned crystals is challenging although several algorithms have been developed for detwinning the X-ray data. Our crystal of the C-terminal domain 2 and 3 of Ski7 (Ski7-D2/3), a key part of non-stop mRNA decay has a perfect twin with the twin operator [h, -h-k, -l]. Many different efforts for phasing with multiple anomalous dispersion techniques using selenomethionine substituted wild-type and mutant proteins were not successful and the phases were obtained through the molecular replacement method using recently reported structure of C-terminal GTPase domain of Ski7 from Saccharomyces cerevisiae. The overall structure of Ski7-D2/3 is very similar to that of the corresponding domain of ribosome-associated GTPases including eIF5B, eEF1α, and eRF3. Domains 2 and 3 form a β-barrel structure containing several structurally deviated long connecting loops. Although the linker between domain 2 and 3 is very flexible, the relative orientation between them is virtually the same among all structures, showing that the Ski7-D2/3 does not show major conformational movement upon contacting with G domain. © 2017 Biodesign
URI
https://pr.ibs.re.kr/handle/8788114/3597
ISSN
2288-6982
Appears in Collections:
Center for Molecular Spectroscopy and Dynamics(분자 분광학 및 동력학 연구단) > Journal Papers (저널논문)
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