This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ok6
From Proteopedia
|
ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE
Overview
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-A 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 (betaalpha)8 barrel fold. Additionally, a crystal structure of the archaeal FBPA covalently bound to dihydroxyacetone phosphate was solved at 2.1-A 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.
About this Structure
1OK6 is a Single protein structure of sequence from Thermoproteus tenax with as ligand. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins., Lorentzen E, Pohl E, Zwart P, Stark A, Russell RB, Knura T, Hensel R, Siebers B, J Biol Chem. 2003 Nov 21;278(47):47253-60. Epub 2003 Aug 26. PMID:12941964
Page seeded by OCA on Thu Feb 21 14:18:38 2008
Categories: Fructose-bisphosphate aldolase | Single protein | Thermoproteus tenax | Hensel, R. | Lorentzen, E. | Pohl, E. | Siebers, B. | Stark, A. | Zwart, P. | GOL | 6-bisphosphate | Aldolase | Archaeal | Fructose 1 | Glycolytic | Lyase | Orthorhombic | Schiff base | Tim barrel
