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Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome.


ABSTRACT: Eukaryotic translation initiation factor eIF5A promotes protein synthesis by resolving polyproline-induced ribosomal stalling. Here, we report a 3.25-Å resolution crystal structure of eIF5A bound to the yeast 80S ribosome. The structure reveals a previously unseen conformation of an eIF5A-ribosome complex and highlights a possible functional link between conformational changes of the ribosome during protein synthesis and the eIF5A-ribosome association.

SUBMITTER: Melnikov S 

PROVIDER: S-EPMC5408928 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome.

Melnikov Sergey S   Mailliot Justine J   Shin Byung-Sik BS   Rigger Lukas L   Yusupova Gulnara G   Micura Ronald R   Dever Thomas E TE   Yusupov Marat M  

Journal of molecular biology 20160516 18


Eukaryotic translation initiation factor eIF5A promotes protein synthesis by resolving polyproline-induced ribosomal stalling. Here, we report a 3.25-Å resolution crystal structure of eIF5A bound to the yeast 80S ribosome. The structure reveals a previously unseen conformation of an eIF5A-ribosome complex and highlights a possible functional link between conformational changes of the ribosome during protein synthesis and the eIF5A-ribosome association. ...[more]

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