Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate

Gardberg, Anna; Abendroth, Jan; Bhandari, Janhavi; Sankaran, Banumathi; Staker, Bart

doi:10.1107/s174430911101894x

Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate

Journal Article · Sat Aug 13 00:00:00 EDT 2011 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/s174430911101894x· OSTI ID:1625811

Gardberg, Anna ^[1]; Abendroth, Jan ^[2]; Bhandari, Janhavi ^[3]; Sankaran, Banumathi ^[4]; Staker, Bart ^[2]

Emerald BioStructures, Bainbridge Island, WA (United States); DOE/OSTI
Emerald BioStructures, Bainbridge Island, WA (United States)
Univ. of Washington, Seattle, WA (United States). School of Medicine. Dept. of Allergy and Infectious Diseases
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)

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 P212121, 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.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1625811

Alternate ID(s):: OSTI ID: 22367599

Journal Information:: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: 9 Vol. 67; ISSN ACSFCL; ISSN 1744-3091

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

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