1OK4

Archaeal fructose 1,6-bisphosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate

Summary for 1OK4

• Entry DOI: 10.2210/pdb1ok4/pdb
• Related: 1OJX 1OK6
• Descriptor: FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS I, 1,3-DIHYDROXYACETONEPHOSPHATE (3 entities in total)
• Functional Keywords: aldolase, fructose 1, 6-bisphosphate, tim barrel, glycolytic, archaeal, lyase
• Biological source: THERMOPROTEUS TENAX
• Total number of polymer chains: 10
• Total formula weight: 289111.22

Authors

Lorentzen, E.,Zwart, P.,Stark, A.,Hensel, R.,Siebers, B.,Pohl, E. (deposition date: 2003-07-17, release date: 2003-09-04, Last modification date: 2023-12-13)

Primary citation

Lorentzen, E.,Pohl, E.,Zwart, P.,Stark, A.,Russell, R.B.,Knura, T.,Hensel, R.,Siebers, B.
Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins.
J. Biol. Chem., 278:47253-47260, 2003

PubMed 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-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.

PubMed: 12941964
DOI: 10.1074/jbc.M305922200

Experimental method

X-RAY DIFFRACTION (2.1 Å)