1ueb
From Proteopedia
(New page: 200px<br /><applet load="1ueb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ueb, resolution 1.65Å" /> '''Crystal structure of...) |
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| - | [[Image:1ueb.jpg|left|200px]]<br /><applet load="1ueb" size=" | + | [[Image:1ueb.jpg|left|200px]]<br /><applet load="1ueb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ueb, resolution 1.65Å" /> | caption="1ueb, resolution 1.65Å" /> | ||
'''Crystal structure of translation elongation factor P from Thermus thermophilus HB8'''<br /> | '''Crystal structure of translation elongation factor P from Thermus thermophilus HB8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Translation elongation factor P (EF-P) stimulates ribosomal | + | 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== | ==About this Structure== | ||
| - | 1UEB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | + | 1UEB is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Hori-Takemoto, C.]] | [[Category: Hori-Takemoto, C.]] | ||
[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sakai, H.]] | [[Category: Sakai, H.]] | ||
[[Category: Sekine, S.]] | [[Category: Sekine, S.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:31 2008'' |
Revision as of 13:23, 21 February 2008
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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 Feb 21 15:23:31 2008
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 genomics
