title: Crystal structure of elongation factor P from Thermus thermophilus HB8.
abstract: 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.
authors.affiliation: RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
authors.forename: Kyoko
authors.initials: K
authors.lastname: Hanawa-Suetsugu
authors.forename: Shun-ichi
authors.initials: S
authors.lastname: Sekine
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Sakai
authors.forename: Chie
authors.initials: C
authors.lastname: Hori-Takemoto
authors.forename: Takaho
authors.initials: T
authors.lastname: Terada
authors.forename: Satoru
authors.initials: S
authors.lastname: Unzai
authors.forename: Jeremy R H
authors.initials: JR
authors.lastname: Tame
authors.forename: Seiki
authors.initials: S
authors.lastname: Kuramitsu
authors.forename: Mikako
authors.initials: M
authors.lastname: Shirouzu
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009690:Nucleic Acid Conformation; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000737:chemistry; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012343:RNA, Transfer / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry; D012270:Ribosomes / Q000378:metabolism; D012996:Solutions; D055672:Static Electricity; D016963:Thermus thermophilus / Q000145:classification* / Q000201:enzymology*; D000097574:Eukaryotic Translation Initiation Factor 5A
chemical_list: D010445:Peptide Elongation Factors; D010448:Peptide Initiation Factors; D012343:RNA, Transfer; D016601:RNA-Binding Proteins; D012996:Solutions; D000097574:Eukaryotic Translation Initiation Factor 5A; C020746:factor EF-P