Lorentzen, E; Pohl, E; Zwart, P; Stark, A; Russell, Rb; Knura, T; Hensel, R; Siebers, B:
Crystal structure of an archaeal class I aldolase and the evolution of (beta alpha)(8) barrel proteins
2003
In: JOURNAL OF BIOLOGICAL CHEMISTRY, Jg. 278 (2003), Heft 47, S. 47253 - 47260
Artikel/Aufsatz in Zeitschrift2003Biologie
Titel:
Crystal structure of an archaeal class I aldolase and the evolution of (beta alpha)(8) barrel proteins
Autor(in):
Lorentzen, E; Pohl, E; Zwart, P; Stark, A; Russell, Rb; Knura, TLSF; Hensel, RLSF; Siebers, BLSF
Erscheinungsjahr
2003

Abstract:

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-Angstrom 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% (R-free 17.9%). The protein forms a dimer of pentamers, consisting of subunits adopting the ubiquitous (betaalpha)(8) barrel fold. Additionally, a crystal structure of the archaeal FBPA covalently bound to dihydroxyacetone phosphate was solved at 2.1-Angstrom 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.