1GVF

Structure of tagatose-1,6-bisphosphate aldolase

Summary for 1GVF

• Entry DOI: 10.2210/pdb1gvf/pdb
• Descriptor: TAGATOSE-BISPHOSPHATE ALDOLASE AGAY, PHOSPHOGLYCOLOHYDROXAMIC ACID, ZINC ION, ... (6 entities in total)
• Functional Keywords: lyase, zinc.
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 64049.16

Authors

Hall, D.R.,Hunter, W.N. (deposition date: 2002-02-11, release date: 2002-06-18, Last modification date: 2024-05-08)

Primary citation

Hall, D.R.,Bond, C.S.,Leonard, G.A.,Watt, C.I.,Berry, A.,Hunter, W.N.
Structure of Tagatose-1,6-Bisphosphate Aldolase; Insight Into Chiral Discrimination, Mechanism and Specificity of Class II Aldolases
J.Biol.Chem., 277:22018-, 2002

PubMed Abstract: Tagatose-1,6-bisphosphate aldolase (TBPA) is a tetrameric class II aldolase that catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate. The high resolution (1.45 A) crystal structure of the Escherichia coli enzyme, encoded by the agaY gene, complexed with phosphoglycolohydroxamate (PGH) has been determined. Two subunits comprise the asymmetric unit, and a crystallographic 2-fold axis generates the functional tetramer. A complex network of hydrogen bonds position side chains in the active site that is occupied by two cations. An unusual Na+ binding site is created using a pi interaction with Tyr183 in addition to five oxygen ligands. The catalytic Zn2+ is five-coordinate using three histidine nitrogens and two PGH oxygens. Comparisons of TBPA with the related fructose-1,6-bisphosphate aldolase (FBPA) identifies common features with implications for the mechanism. Because the major product of the condensation catalyzed by the enzymes differs in the chirality at a single position, models of FBPA and TBPA with their cognate bisphosphate products provide insight into chiral discrimination by these aldolases. The TBPA active site is more open on one side than FBPA, and this contributes to a less specific enzyme. The availability of more space and a wider range of aldehyde partners used by TBPA together with the highly specific nature of FBPA suggest that TBPA might be a preferred enzyme to modify for use in biotransformation chemistry.

PubMed: 11940603
DOI: 10.1074/JBC.M202464200

Experimental method

X-RAY DIFFRACTION (1.45 Å)