1ueb

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spinqualitylabelsall models 1ueb, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of translation elongation factor P from Thermus thermophilus HB8

Overview

Translation elongation factor P (EF-P) stimulates ribosomal, peptidyltransferase activity. EF-P is conserved in bacteria and is, essential for cell viability. Eukarya and Archaea have an EF-P homologue, eukaryotic initiation factor 5A (eIF-5A). In the present study, we, determined the crystal structure of EF-P from Thermus thermophilus HB8 at, a 1.65-A resolution. EF-P consists of three beta-barrel domains (I, II, and III), whereas eIF-5A has only two domains (N and C domains). Domain I, of EF-P is topologically the same as the N domain of eIF-5A. On the other, hand, EF-P domains II and III share the same topology as that of the, eIF-5A C domain, indicating that domains II and III arose by duplication., Intriguingly, the N-terminal half of domain II and the C-terminal half of, domain III of EF-P have sequence homologies to the N- and C-terminal, halves, respectively, of the eIF-5A C domain. The three domains of EF-P, are arranged in an "L" shape, with 65- and 53-A-long arms at an angle of, 95 degrees, which is reminiscent of tRNA. Furthermore, most of the EF-P, protein surface is negatively charged. Therefore, EF-P mimics the tRNA, shape but uses domain topologies different from those of the known, tRNA-mimicry translation factors. Domain I of EF-P has a conserved, positive charge at its tip, like the eIF-5A N domain.

About this Structure

1UEB is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structure of elongation factor P from Thermus thermophilus HB8., Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S, Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9595-600. Epub 2004 Jun 21. PMID:15210970

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