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'''NMR structure of an N-terminal fragment of the eukaryotic initiation factor 5 (eIF5)''' | {{Structure | ||
|PDB= 2g2k |SIZE=350|CAPTION= <scene name='initialview01'>2g2k</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''NMR structure of an N-terminal fragment of the eukaryotic initiation factor 5 (eIF5)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2G2K is a [ | 2G2K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G2K OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors., Conte MR, Kelly G, Babon J, Sanfelice D, Youell J, Smerdon SJ, Proud CG, Biochemistry. 2006 Apr 11;45(14):4550-8. PMID:[http:// | Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors., Conte MR, Kelly G, Babon J, Sanfelice D, Youell J, Smerdon SJ, Proud CG, Biochemistry. 2006 Apr 11;45(14):4550-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16584190 16584190] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: eif5]] | [[Category: eif5]] | ||
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Revision as of 17:59, 20 March 2008
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NMR structure of an N-terminal fragment of the eukaryotic initiation factor 5 (eIF5)
OverviewOverview
Eukaryotic initiation factor 5 (eIF5) plays multiple roles in translation initiation. Its N-terminal domain functions as a GTPase-activator protein (GAP) for GTP bound to eIF2, while its C-terminal region nucleates the interactions between multiple translation factors, including eIF1, which acts to inhibit GTP hydrolysis or P(i) release, and the beta subunit of eIF2. These proteins and the events in which they participate are critical for the accurate recognition of the correct start codon during translation initiation. Here, we report the three-dimensional solution structure of the N-terminal domain of human eIF5, comprising two subdomains, both reminiscent of nucleic-acid-binding modules. The N-terminal subdomain contains the "arginine finger" motif that is essential for GAP function but which, unusually, resides in a partially disordered region of the molecule. This implies that a conformational reordering of this portion of eIF5 is likely to occur upon formation of a competent complex for GTP hydrolysis, following the appropriate activation signal. Interestingly, the N-terminal subdomain of eIF5 reveals an alpha/beta fold structurally similar to both the archaeal orthologue of the beta subunit of eIF2 and, unexpectedly, to eIF1. These results reveal a novel protein fold common to several factors involved in related steps of translation initiation. The implications of these observations are discussed in terms of the mechanism of translation initiation.
About this StructureAbout this Structure
2G2K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors., Conte MR, Kelly G, Babon J, Sanfelice D, Youell J, Smerdon SJ, Proud CG, Biochemistry. 2006 Apr 11;45(14):4550-8. PMID:16584190
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