3TY3

Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe bound to glycyl-glycyl-glycine

3TY3 の概要

• エントリーDOI: 10.2210/pdb3ty3/pdb
• 関連するPDBエントリー: 3TY4
• 分子名称: Probable homoisocitrate dehydrogenase, glycylglycylglycine, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: b-hydroxyacid oxidative decarboxylase, amino-acid biosynthesis, lysine biosynthesis, oxidoreductase
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast)
• 細胞内の位置: Cytoplasm : O14104
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80031.64

構造登録者

Bulfer, S.L.,Hendershot, J.M.,Trievel, R.C. (登録日: 2011-09-23, 公開日: 2011-11-09, 最終更新日: 2023-09-13)

主引用文献

Bulfer, S.L.,Hendershot, J.M.,Trievel, R.C.
Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe.
Proteins, 80:661-666, 2012

PubMed Abstract: Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. The structures illustrate the homology of HICDH with other β-hydroxyacid oxidative decarboxylases and reveal key differences with the active site of Thermus thermophilus HICDH that provide insights into the differences in substrate specificity of these enzymes.

PubMed: 22105743
DOI: 10.1002/prot.23231

実験手法

X-RAY DIFFRACTION (1.85 Å)