CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.420 | Nucleotidyltransferase; domain 5 | |
3.30.420.80 | Ribosomal protein S11 |
Domain Context
CATH Clusters
Superfamily | Ribosomal protein S11 |
Functional Family | 30S ribosomal protein S11 |
Enzyme Information
3.6.5.3 |
Protein-synthesizing GTPase.
based on mapping to UniProt P62263
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)
P62241 |
RS8_HUMAN
Homo sapiens
40S ribosomal protein S8
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PDB Structure
PDB | 5A2Q |
External Links | |
Method | ELECTRON MICROSCOPY |
Organism | |
Primary Citation |
Cryo-Em Structure of Hepatitis C Virus Ires Bound to the Human Ribosome at 3.9 Angstrom Resolution
Nat.Commun.
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