Crystal structure of translation initiation factor 5B from the crenarchaeon Aeropyrum pernix |
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Authors: | Ryo Murakami Tomohiro Miyoshi Toshio Uchiumi Kosuke Ito |
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Institution: | 1. Department of Food and Life Sciences, Graduate School of Science and Technology, Niigata University, Japan;2. Center for Transdisciplinary Research, Niigata University, Japan;3. Department of Biology, Faculty of Science, Niigata University, Japan |
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Abstract: | 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. |
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Keywords: | translational GTPase GTP hydrolysis ribosomal subunit joining X‐ray crystallography molecular evolution |
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