2C7Y

plant enzyme

2C7Y の概要

• エントリーDOI: 10.2210/pdb2c7y/pdb
• 関連するPDBエントリー: 2C7Z
• 分子名称: 3-KETOACYL-COA THIOLASE 2 (2 entities in total)
• 機能のキーワード: fatty acid metabolism, transferase, oxylipin synthesis, lipid synthesis, acyltransferase
• 由来する生物種: ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
• 細胞内の位置: Peroxisome: Q9S7M3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84530.80

構造登録者

Sundaramoorthy, R.,Micossi, E.,Alphey, M.S.,Germain, V.,Bryce, J.H.,Smith, S.M.,Leonard, G.A.,Hunter, W.N. (登録日: 2005-11-30, 公開日: 2006-05-18, 最終更新日: 2024-10-23)

主引用文献

Sundaramoorthy, R.,Micossi, E.,Alphey, M.S.,Germain, V.,Bryce, J.H.,Smith, S.M.,Leonard, G.A.,Hunter, W.N.
The Crystal Structure of a Plant 3-Ketoacyl-Coa Thiolase Reveals the Potential for Redox Control of Peroxisomal Fatty Acid Beta-Oxidation.
J.Mol.Biol., 359:347-, 2006

PubMed Abstract: Crystal structures of peroxisomal Arabidopsis thaliana 3-ketoacyl-CoA thiolase (AtKAT), an enzyme of fatty acid beta-oxidation, are reported. The subunit, a typical thiolase, is a combination of two similar alpha/beta domains capped with a loop domain. The comparison of AtKAT with the Saccharomyces cerevisiae homologue (ScKAT) structure reveals a different placement of subunits within the functional dimers and that a polypeptide segment forming an extended loop around the open catalytic pocket of ScKAT converts to alpha-helix in AtKAT, and occludes the active site. A disulfide is formed between Cys192, on this helix, and Cys138, a catalytic residue. Access to Cys138 is determined by the structure of this polypeptide segment. AtKAT represents an oxidized, previously unknown inactive form, whilst ScKAT is the reduced and active enzyme. A high level of sequence conservation is observed, including Cys192, in eukaryotic peroxisomal, but not mitochondrial or prokaryotic KAT sequences, for this labile loop/helix segment. This indicates that KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation with redox regulation.

PubMed: 16630629
DOI: 10.1016/J.JMB.2006.03.032

実験手法

X-RAY DIFFRACTION (2.1 Å)