2FJK

Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus

2FJK の概要

• エントリーDOI: 10.2210/pdb2fjk/pdb
• 分子名称: Fructose-bisphosphate aldolase, 1,3-DIHYDROXYACETONEPHOSPHATE (3 entities in total)
• 機能のキーワード: beta-alpha-barrels, lyase
• 由来する生物種: Thermus caldophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 134324.51

構造登録者

Lee, J.H.,Im, Y.J.,Rho, S.-H.,Kim, M.-K.,Kang, G.B.,Eom, S.H. (登録日: 2006-01-03, 公開日: 2006-08-08, 最終更新日: 2024-10-16)

主引用文献

Lee, J.H.,Bae, J.,Kim, D.,Choi, Y.,Im, Y.J.,Koh, S.,Kim, J.S.,Kim, M.-K.,Kang, G.B.,Hong, S.-I.,Lee, D.-S.,Eom, S.H.
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus
Biochem.Biophys.Res.Commun., 347:616-625, 2006

PubMed Abstract: 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.

PubMed: 16843441
DOI: 10.1016/j.bbrc.2006.06.139

実験手法

X-RAY DIFFRACTION (2.2 Å)