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  Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases

Kowalinski, E., Schuller, A., Green, R., & Conti, E. (2015). Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases. STRUCTURE, 23(7), 1336-1343. doi:10.1016/j.str.2015.04.018.

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 Creators:
Kowalinski, Eva1, Author           
Schuller, Anthony2, Author
Green, Rachel2, Author
Conti, Elena1, Author           
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1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              

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Free keywords: MESSENGER-RNA DECAY; ELONGATION-FACTOR TU; QUALITY-CONTROL SYSTEMS; FACTOR EF-TU; NO-GO DECAY; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; MAMMALIAN-CELLS; COMPLEX; DEGRADATION
 Abstract: Ski7 is a cofactor of the cytoplasmic exosome in budding yeast, functioning in both mRNA turnover and non-stop decay (NSD), a surveillance pathway that degrades faulty mRNAs lacking a stop codon. The C-terminal region of Ski7 (Ski7(C)) shares overall sequence similarity with the translational GTPase (trGTPase) Hbs1, but whether Ski7 has retained the properties of a trGTPase is unclear. Here, we report the high-resolution structures of Ski7(C) bound to either intact guanosine triphosphate (GTP) or guanosine diphosphate-Pi. The individual domains of Ski7(C) adopt the conformation characteristic of active trGTPases. Furthermore, the nucleotide-binding site of Ski7(C) shares similar features compared with active trGTPases, notably the presence of a characteristic monovalent cation. However, a suboptimal polar residue at the putative catalytic site and an unusual polar residue that interacts with the g-phosphate of GTP distinguish Ski7 from other trGTPases, suggesting it might function rather as a GTP-binding protein than as a GTP-hydrolyzing enzyme.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000360312200020
DOI: 10.1016/j.str.2015.04.018
 Degree: -

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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 23 (7) Sequence Number: - Start / End Page: 1336 - 1343 Identifier: ISSN: 0969-2126