1U0L

Crystal structure of YjeQ from Thermotoga maritima

Summary for 1U0L

• Entry DOI: 10.2210/pdb1u0l/pdb
• Descriptor: Probable GTPase engC, ZINC ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: gtpase, permutation, ob-fold, zinc-finger, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, hydrolase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 3
• Total formula weight: 103621.61

Authors

Shin, D.H.,Lou, Y.,Jaru, J.,Kim, R.,Yokota, H.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2004-07-13, release date: 2004-09-07, Last modification date: 2024-02-14)

Primary citation

Shin, D.H.,Lou, Y.,Jancarik, J.,Yokota, H.,Kim, R.,Kim, S.H.
Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain
Proc.Natl.Acad.Sci.Usa, 101:13198-13203, 2004

PubMed Abstract: 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.

PubMed: 15331784
DOI: 10.1073/pnas.0405202101

Experimental method

X-RAY DIFFRACTION (2.8 Å)