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1ueb
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Categories: Single protein | Thermus thermophilus | Hanawa-Suetsugu, K. | Hori-Takemoto, C. | Kuramitsu, S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sakai, H. | Sekine, S. | Shirouzu, M. | Terada, T. | Yokoyama, S. | Beta barrel | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ueb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ueb OCA], [http://www.ebi.ac.uk/pdbsum/1ueb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ueb RCSB]</span> | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
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Revision as of 21:09, 30 March 2008
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| , resolution 1.65Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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