1UEB

Crystal structure of translation elongation factor P from Thermus thermophilus HB8

Summary for 1UEB

• Entry DOI: 10.2210/pdb1ueb/pdb
• Descriptor: elongation factor P (2 entities in total)
• Functional Keywords: beta barrel, riken structural genomics/proteomics initiative, rsgi, structural genomics, rna binding protein
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: Q76G20
• Total number of polymer chains: 2
• Total formula weight: 40494.02

Authors

Hanawa-Suetsugu, K.,Sekine, S.,Sakai, H.,Hori-Takemoto, C.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-05-09, release date: 2004-05-25, Last modification date: 2023-12-27)

Primary citation

Hanawa-Suetsugu, K.,Sekine, S.,Sakai, H.,Hori-Takemoto, C.,Terada, T.,Unzai, S.,Tame, J.R.H.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.
Crystal structure of elongation factor P from Thermus thermophilus HB8
Proc.Natl.Acad.Sci.USA, 101:9595-9600, 2004

PubMed 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.

PubMed: 15210970
DOI: 10.1073/pnas.0308667101

Experimental method

X-RAY DIFFRACTION (1.65 Å)