3MMT
Crystal structure of fructose bisphosphate aldolase from Bartonella henselae, bound to fructose bisphosphate
Summary for 3MMT
| Entry DOI | 10.2210/pdb3mmt/pdb |
| Related | 3KX6 3MBD 3MBF |
| Descriptor | Fructose-bisphosphate aldolase, 1,6-FRUCTOSE DIPHOSPHATE (LINEAR FORM) (3 entities in total) |
| Functional Keywords | ssgcid, aldolase, structural genomics, seattle structural genomics center for infectious disease, hydrolase |
| Biological source | Bartonella henselae (Rochalimaea henselae) |
| Total number of polymer chains | 4 |
| Total formula weight | 151584.92 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-04-20, release date: 2010-05-19, Last modification date: 2024-11-20) |
| Primary citation | Gardberg, A.,Abendroth, J.,Bhandari, J.,Sankaran, B.,Staker, B. Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate. Acta Crystallogr.,Sect.F, 67:1051-1054, 2011 Cited by PubMed 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. PubMed: 21904049DOI: 10.1107/S174430911101894X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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