1K5H

1-deoxy-D-xylulose-5-phosphate reductoisomerase

1K5H の概要

• エントリーDOI: 10.2210/pdb1k5h/pdb
• 分子名称: 1-deoxy-D-xylulose-5-phosphate reductoisomerase (2 entities in total)
• 機能のキーワード: alpha-helix, beta-barrel, dinucleotide binding motif, variable loop, induced fit, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 130295.64

構造登録者

Reuter, K.,Sanderbrand, S.,Jomaa, H.,Wiesner, J.,Steinbrecher, I.,Beck, E.,Hintz, M.,Klebe, G.,Stubbs, M.T. (登録日: 2001-10-10, 公開日: 2002-02-27, 最終更新日: 2024-10-30)

主引用文献

Reuter, K.,Sanderbrand, S.,Jomaa, H.,Wiesner, J.,Steinbrecher, I.,Beck, E.,Hintz, M.,Klebe, G.,Stubbs, M.T.
Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis.
J.Biol.Chem., 277:5378-5384, 2002

PubMed Abstract: We have solved the 2.5-A crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, an enzyme involved in the mevalonate-independent 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis. The structure reveals that the enzyme is present as a homodimer. Each monomer displays a V-like shape and is composed of an amino-terminal dinucleotide binding domain, a connective domain, and a carboxyl-terminal four-helix bundle domain. The connective domain is responsible for dimerization and harbors most of the active site. The strictly conserved acidic residues Asp(150), Glu(152), Glu(231), and Glu(234) are clustered at the putative active site and are probably involved in the binding of divalent cations mandatory for enzyme activity. The connective and four-helix bundle domains show significant mobility upon superposition of the dinucleotide binding domains of the three conformational states present in the asymmetric unit of the crystal. A still more pronounced flexibility is observed for a loop spanning residues 186 to 216, which adopts two completely different conformations within the three protein conformers. A possible involvement of this loop in an induced fit during substrate binding is discussed.

PubMed: 11741911
DOI: 10.1074/jbc.M109500200

実験手法

X-RAY DIFFRACTION (2.5 Å)