CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.40 | Beta Barrel | |
2.40.30 | Elongation Factor Tu (Ef-tu); domain 3 | |
2.40.30.10 | Translation factors |
Domain Context
CATH Clusters
Superfamily | Translation factors |
Functional Family | Eukaryotic translation initiation factor 5B |
Enzyme Information
3.6.5.3 |
Protein-synthesizing GTPase.
based on mapping to UniProt P39730
GTP + H(2)O = GDP + phosphate.
-!- This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. -!- In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyzes it in prokaryotes. -!- In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. -!- In the elongation phase, the GTP-hydrolyzing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1-alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). -!- EF-Tu and EF-1-alpha catalyze binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyze the translocation of peptidyl-tRNA from the A-site to the P-site. -!- GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs. -!- Formerly EC 3.6.1.48.
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UniProtKB Entries (1)
P38912 |
IF1A_YEAST
Saccharomyces cerevisiae S288C
Eukaryotic translation initiation factor 1A
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PDB Structure
PDB | 3WBK |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
X-ray structures of eIF5B and the eIF5B-eIF1A complex: the conformational flexibility of eIF5B is restricted on the ribosome by interaction with eIF1A
Acta Crystallogr.,Sect.D
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