3R1M

Structure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)

Summary for 3R1M

• Entry DOI: 10.2210/pdb3r1m/pdb
• Related: 1UMG
• Descriptor: Putative uncharacterized protein ST0318, 1,3-DIHYDROXYACETONEPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: sulfolobus fructose-1, 6-bisphosphatase-like fold, hydrolase/aldolase, mg binding, metal binding protein
• Biological source: Sulfolobus tokodaii
• Total number of polymer chains: 1
• Total formula weight: 43121.12

Authors

Fushinobu, S.,Nishimasu, H.,Hattori, D.,Song, H.-J.,Wakagi, T. (deposition date: 2011-03-10, release date: 2011-10-12, Last modification date: 2024-10-16)

Primary citation

Fushinobu, S.,Nishimasu, H.,Hattori, D.,Song, H.-J.,Wakagi, T.
Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase.
Nature, 478:538-541, 2011

PubMed Abstract: Enzymes catalyse specific reactions and are essential for maintaining life. Although some are referred to as being bifunctional, they consist of either two distinct catalytic domains or a single domain that displays promiscuous substrate specificity. Thus, one enzyme active site is generally responsible for one biochemical reaction. In contrast to this conventional concept, archaeal fructose-1,6-bisphosphate (FBP) aldolase/phosphatase (FBPA/P) consists of a single catalytic domain, but catalyses two chemically distinct reactions of gluconeogenesis: (1) the reversible aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to FBP; (2) the dephosphorylation of FBP to fructose-6-phosphate (F6P). Thus, FBPA/P is fundamentally different from ordinary enzymes whose active sites are responsible for a specific reaction. However, the molecular mechanism by which FBPA/P achieves its unusual bifunctionality remains unknown. Here we report the crystal structure of FBPA/P at 1.5-Å resolution in the aldolase form, where a critical lysine residue forms a Schiff base with DHAP. A structural comparison of the aldolase form with a previously determined phosphatase form revealed a dramatic conformational change in the active site, demonstrating that FBPA/P metamorphoses its active-site architecture to exhibit dual activities. Thus, our findings expand the conventional concept that one enzyme catalyses one biochemical reaction.

PubMed: 21983966
DOI: 10.1038/nature10457

Experimental method

X-RAY DIFFRACTION (1.5 Å)