1ueb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ueb.jpg|left|200px]] | [[Image:1ueb.jpg|left|200px]] | ||
'''Crystal structure of translation elongation factor P from Thermus thermophilus HB8''' | {{Structure | ||
|PDB= 1ueb |SIZE=350|CAPTION= <scene name='initialview01'>1ueb</scene>, resolution 1.65Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of translation elongation factor P from Thermus thermophilus HB8''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1UEB is a [ | 1UEB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UEB OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15210970 15210970] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
| Line 25: | Line 34: | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:30:52 2008'' | ||
Revision as of 12:30, 20 March 2008
| |||||||||||||
| 1ueb, resolution 1.65Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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
Page seeded by OCA on Thu Mar 20 14:30:52 2008
