Crystal Structure of Hyperthermophilic Archaeal Initiation Factor 5A: A Homologue of Eukaryotic Initiation Factor 5A (eIF-5A)
| Autor: | Min Yao, Makoto Kimura, Isao Tanaka, Shingo Kikukawa, Akiko Ohsawa |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Methanococcus Stereochemistry Molecular Sequence Data Crystallography X-Ray Biochemistry Pyrococcus horikoshii chemistry.chemical_compound Oligosaccharide binding Peptide Initiation Factors Eukaryotic initiation factor Initiation factor Molecular replacement Amino Acid Sequence Molecular Biology Hypusine Binding Sites Sequence Homology Amino Acid biology Lysine RNA-Binding Proteins RNA General Medicine biology.organism_classification Protein Structure Tertiary chemistry Structural Homology Protein |
| Zdroj: | Journal of Biochemistry. 133:75-81 |
| ISSN: | 0021-924X |
| DOI: | 10.1093/jb/mvg011 |
| Popis: | Eukaryotic initiation factor 5A (eIF-5A) is ubiquitous in eukaryotes and archaebacteria and is essential for cell proliferation and survival. The crystal structure of the eIF-5A homologue (PhoIF-5A) from a hyperthermophilic archaebacterium Pyrococcus horikoshii OT3 was determined at 2.0 A resolution by the molecular replacement method. PhoIF-5A is predominantly composed of beta-strands comprising two distinct folding domains, an N-domain (residues 1-69) and a C-domain (residues 72-138), connected by a short linker peptide (residues 70-71). The N-domain has an SH3-like barrel, while the C-domain folds in an (oligonucleotide/oligosaccharide binding) OB fold. Comparison of the structure of PhoIF-5A with those of archaeal homologues from Methanococcus jannaschii and Pyrobaculum aerophilum showed that the N-domains could be superimposed with root mean square deviation (rmsd) values of 0.679 and 0.624 A, while the C-domains gave higher values of 1.824 and 1.329 A, respectively. Several lines of evidence suggest that eIF-5A functions as a biomodular protein capable of interacting with protein and nucleic acid. The surface representation of electrostatic potential shows that PhoIF-5A has a concave surface with positively charged residues between the N- and C-domains. In addition, a flexible long hairpin loop, L1 (residues 33-41), with a hypusine modification site is positively charged, protruding from the N-domain. In contrast, the opposite side of the concave surface at the C-domain is mostly negatively charged. These findings led to the speculation that the concave surface and loop L1 at the N-domain may be involved in RNA binding, while the opposite side of the concave surface in the C-domain may be involved in protein interaction. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|