Lorentzen, E. and Pohl, E. and Zwart, P. and Stark, A. and Russell, R. B. and Knura, T. and Hensel, R. and Siebers, B. (2003) 'Crystal structure of an archaeal class I aldolase and the evolution of (beta alpha)(8) barrel proteins.', Journal of biological chemistry., 278 (47). pp. 47253-47260.
Fructose-1,6-bisphosphate aldolase (FBPA) catalyzes the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in the glycolytic pathway. FBPAs from archaeal organisms have recently been identified and characterized as a divergent family of proteins. Here, we report the first crystal structure of an archaeal FBPA at 1.9-Å resolution. The structure of this 280-kDa protein complex was determined using single wavelength anomalous dispersion followed by 10-fold non-crystallographic symmetry averaging and refined to an R-factor of 14.9% (Rfree 17.9%). The protein forms a dimer of pentamers, consisting of subunits adopting the ubiquitous ()8 barrel fold. Additionally, a crystal structure of the archaeal FBPA covalently bound to dihydroxyacetone phosphate was solved at 2.1-Å resolution. Comparison of the active site residues with those of classical FBPAs, which share no significant sequence identity but display the same overall fold, reveals a common ancestry between these two families of FBPAs. Structural comparisons, furthermore, establish an evolutionary link to the triosephosphate isomerases, a superfamily hitherto considered independent from the superfamily of aldolases.
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|Publisher Web site:||http://dx.doi.org/10.1074/jbc.M305922200|
|Record Created:||16 Jan 2008|
|Last Modified:||08 Apr 2009 16:36|
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