1wb3
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CRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METHANOCOCCUS MARIPALUDIS IN COMPLEX WITH THE GTP ANALOGUE GPPNHP
OverviewOverview
In all three kingdoms of life, SelB is a specialized translation, elongation factor responsible for the cotranslational incorporation of, selenocysteine into proteins by recoding of a UGA stop codon in the, presence of a downstream mRNA hairpin loop. Here, we present the X-ray, structures of SelB from the archaeon Methanococcus maripaludis in the, apo-, GDP- and GppNHp-bound form and use mutational analysis to, investigate the role of individual amino acids in its aminoacyl-binding, pocket. All three SelB structures reveal an EF-Tu:GTP-like domain, arrangement. Upon binding of the GTP analogue GppNHp, a conformational, change of the Switch 2 region in the GTPase domain leads to the exposure, of SelB residues involved in clamping the 5' phosphate of the tRNA. A, conserved extended loop in ... [(full description)]
About this StructureAbout this Structure
1WB3 is a [Single protein] structure of sequence from [Methanococcus maripaludis] with MG, SO4, GNP and DXC as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors., Leibundgut M, Frick C, Thanbichler M, Bock A, Ban N, EMBO J. 2005 Jan 12;24(1):11-22. Epub 2004 Dec 23. PMID:15616587
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