1QO5

Fructose 1,6-bisphosphate Aldolase from Human Liver Tissue

1QO5 の概要

• エントリーDOI: 10.2210/pdb1qo5/pdb
• 関連するPDBエントリー: 1ALD
• 分子名称: FRUCTOSE-BISPHOSPHATE ALDOLASE B, SULFATE ION (3 entities in total)
• 機能のキーワード: aldolase, tim barrel, glycolytic enzyme, lyase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 710438.86

構造登録者

Dalby, A.R.,Littlechild, J.A. (登録日: 1999-11-03, 公開日: 2000-11-05, 最終更新日: 2023-12-13)

主引用文献

Dalby, A.R.,Tolan, D.R.,Littlechild, J.A.
The Structure of Human Liver Fructose-1,6-Bisphosphate Aldolase
Acta Crystallogr.,Sect.D, 57:1526-, 2001

PubMed Abstract: The X-ray crystallographic structure of the human liver isozyme of fructose-1,6-bisphosphate aldolase has been determined by molecular replacement using a tetramer of the human muscle isozyme as a search model. The liver aldolase (B isozyme) crystallized in space group C2, with unit-cell parameters a = 291.1, b = 489.8, c = 103.4 A, alpha = 90, beta = 103.6, gamma = 90 degrees. These large unit-cell parameters result from the presence of 18 subunits in the asymmetric unit: four catalytic tetramers and a dimer from a fifth tetramer positioned on the twofold crystallographic axis. This structure provides further insight into the factors affecting isozyme specificity. It reveals small differences in secondary structure that occur in regions previously determined to be isozyme specific. Two of these regions are at the solvent-exposed enzyme surface away from the active site of the enzyme. The most significant changes are in the flexible C-terminal region of the enzyme, where there is an insertion of an extra alpha-helix. Point mutations of the human liver aldolase are responsible for the disease hereditary fructose intolerance. Sequence information is projected onto the new crystal structure in order to indicate how these mutations bring about reduced enzyme activity and affect structural stability.

PubMed: 11679716
DOI: 10.1107/S0907444901012719

実験手法

X-RAY DIFFRACTION (2.5 Å)