1HNO

CRYSTAL STRUCTURE OF PEROXISOMAL DELTA3-DELTA2-ENOYL-COA ISOMERASE FROM SACCHAROMYCES CEREVISIAE

1HNO の概要

• エントリーDOI: 10.2210/pdb1hno/pdb
• 関連するPDBエントリー: 1HNU
• 分子名称: D3,D2-ENOYL COA ISOMERASE ECI1, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: alpha/beta, unliganded, isomerase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Peroxisome: Q05871
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31842.50

構造登録者

Mursula, A.M.,van Aalten, D.M.F.,Hiltunen, J.K.,Wierenga, R.K. (登録日: 2000-12-08, 公開日: 2001-06-20, 最終更新日: 2024-04-03)

主引用文献

Mursula, A.M.,van Aalten, D.M.,Hiltunen, J.K.,Wierenga, R.K.
The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase.
J.Mol.Biol., 309:845-853, 2001

PubMed Abstract: The active-site geometry of the first crystal structure of a Delta(3)-Delta(2)-enoyl-coenzyme A (CoA) isomerase (the peroxisomal enzyme from the yeast Saccharomyces cerevisiae) shows that only one catalytic base, Glu158, is involved in shuttling the proton from the C2 carbon atom of the substrate, Delta(3)-enoyl-CoA, to the C4 atom of the product, Delta(2)-enoyl-CoA. Site-directed mutagenesis has been performed to confirm that this glutamate residue is essential for catalysis. This Delta(3)-Delta(2)-enoyl-CoA isomerase is a hexameric enzyme, consisting of six identical subunits. It belongs to the hydratase/isomerase superfamily of enzymes which catalyze a wide range of CoA-dependent reactions. The members of the hydratase/ isomerase superfamily have only a low level of sequence identity. Comparison of the crystal structure of the Delta(3)-Delta(2)-enoyl-CoA isomerase with the other structures of this superfamily shows only one region of large structural variability, which is in the second turn of the spiral fold and which is involved in defining the shape of the binding pocket.

PubMed: 11399063
DOI: 10.1006/jmbi.2001.4671

実験手法

X-RAY DIFFRACTION (2.5 Å)