1fl9
THE YJEE PROTEIN
|
OverviewOverview
A hypothetical protein encoded by the gene YjeE of Haemophilus influenzae, was selected as part of a structural genomics project for X-ray analysis, to assist with the functional assignment. The protein is considered, essential to bacteria because the gene is present in virtually all, bacterial genomes but not in those of archaea or eukaryotes. The amino, acid sequence shows no homology to other proteins except for the presence, of the Walker A motif G-X-X-X-X-G-K-T that indicates the possibility of a, nucleotide-binding protein. The YjeE protein was cloned, expressed, and, the crystal structure determined by the MAD method at 1.7-A resolution., The protein has a nucleotide-binding fold with a four-stranded parallel, beta-sheet flanked by antiparallel beta-strands on each side. The topology, of the beta-sheet is unique among P-loop proteins and has features of, different families of enzymes. Crystallization of YjeE in the presence of, ATP and Mg2+ resulted in the structure with ADP bound in the P-loop. The, ATPase activity of YjeE was confirmed by kinetic measurements. The, distribution of conserved residues suggests that the protein may work as a, "molecular switch" triggered by ATP hydrolysis. The phylogenetic pattern, of YjeE suggests its involvement in cell wall biosynthesis.
About this StructureAbout this Structure
1FL9 is a Single protein structure of sequence from Haemophilus influenzae with HG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesis., Teplyakov A, Obmolova G, Tordova M, Thanki N, Bonander N, Eisenstein E, Howard AJ, Gilliland GL, Proteins. 2002 Aug 1;48(2):220-6. PMID:12112691
Page seeded by OCA on Tue Nov 20 15:00:52 2007