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Crystal structure of translation initiation factor 5B from the crenarchaeon Aeropyrum pernix
Author(s) -
Murakami Ryo,
Miyoshi Tomohiro,
Uchiumi Toshio,
Ito Kosuke
Publication year - 2016
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25009
Subject(s) - archaea , initiation factor , biology , eukaryotic translation , protein subunit , eif2 , gtpase , translation (biology) , ribosomal rna , domain (mathematical analysis) , release factor , eukaryotic initiation factor , genetics , microbiology and biotechnology , computational biology , evolutionary biology , ribosome , rna , gene , messenger rna , mathematical analysis , mathematics
Initiation factor 5B (IF5B) is a universally conserved translational GTPase that catalyzes ribosomal subunit joining. In eukaryotes, IF5B directly interacts via a groove in its domain IV with initiation factor 1A (IF1A), another universally conserved initiation factor, to accomplish efficient subunit joining. Here, we have determined the first structure of a crenarchaeal IF5B, which revealed that the archaea‐specific region of IF5B (helix α15) binds and occludes the groove of domain IV. Therefore, archaeal IF5B cannot access IF1A in the same manner as eukaryotic IF5B. This fact suggests that different relationships between IF5B and IF1A exist in archaea and eukaryotes. Proteins 2016; 84:712–717. © 2016 Wiley Periodicals, Inc.