1u0l | pdb_00001u0l

File:1u0l.jpg

spinqualitylabelsall models 1u0l, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Crystal structure of YjeQ from Thermotoga maritima

Overview

We have determined the crystal structure of the GDP complex of the YjeQ, protein from Thermotoga maritima (TmYjeQ), a member of the YjeQ GTPase, subfamaily. TmYjeQ, a homologue of Escherichia coli YjeQ, which is known, to bind to the ribosome, is composed of three domains: an N-terminal, oligonucleotide/oligosaccharide-binding fold domain, a central GTPase, domain, and a C-terminal zinc-finger domain. The crystal structure of, TmYjeQ reveals two interesting domains: a circularly permutated GTPase, domain and an unusual zinc-finger domain. The binding mode of GDP in the, GTPase domain of TmYjeQ is similar to those of GDP or GTP analogs in ras, proteins, a prototype GTPase. The N-terminal, oligonucleotide/oligosaccharide-binding fold domain, together with the, GTPase domain, forms the extended RNA-binding site. The C-terminal domain, has an unusual zinc-finger motif composed of Cys-250, Cys-255, Cys-263, and His-257, with a remote structural similarity to a portion of a, DNA-repair protein, rad51 fragment. The overall structural features of, TmYjeQ make it a good candidate for an RNA-binding protein, which is, consistent with the biochemical data of the YjeQ subfamily in binding to, the ribosome.

About this Structure

1U0L is a Single protein structure of sequence from Thermotoga maritima with ZN and GDP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain., Shin DH, Lou Y, Jancarik J, Yokota H, Kim R, Kim SH, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13198-203. Epub 2004 Aug 26. PMID:15331784

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