Abstract
Fructose bisphosphate aldolase (FBPA) enzymes have been found in a broad range of eukaryotic and prokaryotic organisms. FBPA catalyses the cleavage of fructose 1,6-bisphosphate into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The SSGCID has reported several FBPA structures from pathogenic sources, including the bacterium Brucella melitensis and the protozoan Babesia bovis. Bioinformatic analysis of the Bartonella henselae genome revealed an FBPA homolog. The B. henselae FBPA enzyme was recombinantly expressed and purified for X-ray crystallographic studies. The purified enzyme crystallized in the apo form but failed to diffract; however, well diffracting crystals could be obtained by cocrystallization in the presence of the native substrate fructose 1,6-bisphosphate. A data set to 2.35 Å resolution was collected from a single crystal at 100 K. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=72.39, b=127.71, c=157.63 Å. The structure was refined to a final free R factor of 22.2%. The structure shares the typical barrel tertiary structure and tetrameric quaternary structure reported for previous FBPA structures and exhibits the same Schiff base in the active site.
Highlights
The Seattle Structural Genomics Center for Infectious Disease (SSGCID) is one of two consortia funded by NIAID to apply genome-scale approaches to the solution of protein structures from biodefense organisms, as well as those causing emerging and reemerging diseases
B. henselae fructose bisphosphate aldolase (BhFBPA) crystallized with four monomers in the asymmetric unit (50% solvent content; Matthews coefficient VM = 2.45 A 3 DaÀ1; Matthews, 1968)
The crystal structure of fructose bisphosphate aldolase from B. henselae was determined in complex with its reactant at 2.35 Aresolution
Summary
The Seattle Structural Genomics Center for Infectious Disease (SSGCID) is one of two consortia funded by NIAID to apply genome-scale approaches to the solution of protein structures from biodefense organisms, as well as those causing emerging and reemerging diseases. In its first three and a half years, the SSGCID has submitted $350 protein structures to the Protein Data Bank (PDB) and is on track to solve a further 100 per year going forward. For several organisms, this represents the majority of PDB submissions during this time, including 100% of the structures for Ehrlichia, Anaplasma and Burkholderia.
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