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Crystal structure of an archaeal class I aldolase and the evolution of (beta alpha)(8) barrel proteins.

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.

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-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.

Item Type:Article
Additional Information:
Full text:Full text not available from this repository.
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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