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1iz6

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[[Image:1iz6.jpg|left|200px]]
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{{STRUCTURE_1iz6| PDB=1iz6 | SCENE= }}
{{STRUCTURE_1iz6| PDB=1iz6 | SCENE= }}
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'''Crystal Structure of Translation Initiation Factor 5A from Pyrococcus Horikoshii'''
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===Crystal Structure of Translation Initiation Factor 5A from Pyrococcus Horikoshii===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12761201 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12761201}}
==About this Structure==
==About this Structure==
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[[Category: Ob fold]]
[[Category: Ob fold]]
[[Category: Sh3-like barrel]]
[[Category: Sh3-like barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:36:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:15:27 2008''

Revision as of 11:15, 1 July 2008

Template:STRUCTURE 1iz6

Crystal Structure of Translation Initiation Factor 5A from Pyrococcus Horikoshii

Template:ABSTRACT PUBMED 12761201

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. 2003 Jan;133(1):75-81. PMID:12761201

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