1jal
YCHF PROTEIN (HI0393)
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OverviewOverview
The bacterial protein encoded by the gene ychF is 1 of 11 universally, conserved GTPases and the only one whose function is unknown. The crystal, structure determination of YchF was sought to help with the functional, assignment of the protein. The YchF protein from Haemophilus influenzae, was cloned and expressed, and the crystal structure was determined at 2.4, A resolution. The polypeptide chain is folded into three domains. The, N-terminal domain has a mononucleotide binding fold typical for the P-loop, NTPases. An 80-residue domain next to it has a pronounced alpha-helical, coiled coil. The C-terminal domain features a six-stranded half-barrel, that curves around an alpha-helix. The crablike three-domain structure of, YchF suggests the binding site for a double-stranded nucleic acid in the, cleft between the domains. The structure of the putative GTP-binding site, is consistent with the postulated guanine specificity of the protein., Fluorescence measurements have demonstrated the ability of YchF to bind a, double-stranded nucleic acid and GTP. Taken together with other, experimental data and genomic analysis, these results suggest that YchF, may be part of a nucleoprotein complex and may function as a GTP-dependent, translation factor.
About this StructureAbout this Structure
1JAL is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid., Teplyakov A, Obmolova G, Chu SY, Toedt J, Eisenstein E, Howard AJ, Gilliland GL, J Bacteriol. 2003 Jul;185(14):4031-7. PMID:12837776
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