1iz6
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(New page: 200px<br /><applet load="1iz6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iz6, resolution 2.0Å" /> '''Crystal Structure of ...)
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Revision as of 15:40, 20 November 2007
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Crystal Structure of Translation Initiation Factor 5A from Pyrococcus Horikoshii
Overview
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.
About this Structure
1IZ6 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
Reference
Crystal structure of hyperthermophilic archaeal initiation factor 5A: a homologue of eukaryotic initiation factor 5A (eIF-5A)., Yao M, Ohsawa A, Kikukawa S, Tanaka I, Kimura M, J Biochem (Tokyo). 2003 Jan;133(1):75-81. PMID:12761201
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