2fjk
From Proteopedia
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Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus
Overview
It was recently established that fructose-1,6-bisphosphate (FBP) aldolase, (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II, aldolases, are highly specific for the diastereoselective synthesis of FBP, and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone, phosphate (DHAP), respectively. In this paper, we report on a FBA from the, thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP, from C(3) substrates. Moreover, the FBP:TBP ratio could be adjusted by, manipulating the concentrations of G3P and DHAP. This is the first native, FBA known to show dual diastereoselectivity among the FBAs and TBAs, characterized thus far. To explain the behavior of this enzyme, the X-ray, crystal structure of the Tca FBA in complex with DHAP was determined at, 2.2A resolution. It appears that as a result of alteration of five G3P, binding residues, the substrate binding cavity of Tca FBA has a greater, volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate, (PGH) and TBA-PGH complexes. We suggest that this steric difference, underlies the difference in the diastereoselectivities of these class II, aldolases.
About this Structure
2FJK is a Single protein structure of sequence from Thermus caldophilus with 13P as ligand. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Full crystallographic information is available from OCA.
Reference
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus., Lee JH, Bae J, Kim D, Choi Y, Im YJ, Koh S, Kim JS, Kim MK, Kang GB, Hong SI, Lee DS, Eom SH, Biochem Biophys Res Commun. 2006 Sep 1;347(3):616-25. Epub 2006 Jul 5. PMID:16843441
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