1ueb

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{{STRUCTURE_1ueb| PDB=1ueb | SCENE= }}
{{STRUCTURE_1ueb| PDB=1ueb | SCENE= }}
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'''Crystal structure of translation elongation factor P from Thermus thermophilus HB8'''
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===Crystal structure of translation elongation factor P from Thermus thermophilus HB8===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15210970 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15210970}}
==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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Revision as of 07:35, 28 July 2008

Image:1ueb.png

Template:STRUCTURE 1ueb

Crystal structure of translation elongation factor P from Thermus thermophilus HB8

Template:ABSTRACT PUBMED 15210970

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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