4FBP

CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)

4FBP の概要

• エントリーDOI: 10.2210/pdb4fbp/pdb
• 分子名称: FRUCTOSE 1,6-BISPHOSPHATASE, ADENOSINE MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: hydrolase (phosphoric monoester)
• 由来する生物種: Sus scrofa (pig)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 147400.90

構造登録者

Ke, H.,Zhang, Y.,Liang, J.-Y.,Lipscomb, W.N. (登録日: 1991-02-11, 公開日: 1992-07-15, 最終更新日: 2024-02-28)

主引用文献

Ke, H.M.,Liang, J.Y.,Zhang, Y.P.,Lipscomb, W.N.
Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form).
Biochemistry, 30:4412-4420, 1991

PubMed Abstract: A structure of the neutral form of fructose-1,6-bisphosphatase complexed with AMP has been determined by the molecular replacement method and refined at a 2.5-A resolution to a crystallographic R factor of 0.169. The root-mean-square errors of the structure from standard geometry are 0.013 A for bond lengths and 2.99 degrees for bond angles. Comparison of the AMP complex with the F6P complex shows that dimer C3-C4 twists about 19 degrees about a molecular 2-fold axis when dimers C1-C2 of the R and T forms of the enzyme are superimposed one another and that a slight shift of about 1 A of the AMP domain partially compensates this twist. The R to T transition of the enzyme does not significantly change the conformation of the F6P-binding site. However, residues at the divalent metal site and the AMP site show significant positional shifts. If these results can be extended to substrate in place of F6P, they suggest that regulation of the enzyme by AMP may occur partly through effects on metal-ion affinity or position. AMP binds to the same sites of the T and R forms, but only half-occupancy was observed in the alkaline R form. Sequential binding of AMP, at least in pairs, is suggested as the unligated R form is converted to the T form. Two possible pathways are suggested for allosteric communication over about 28 A between the AMP site and the active site: one via helices H1, H2, and H3 and another via the eight-stranded beta-sheet.(ABSTRACT TRUNCATED AT 250 WORDS)

PubMed: 1850623
DOI: 10.1021/bi00232a007

実験手法

X-RAY DIFFRACTION (2.5 Å)