1TKL

Yeast Oxygen-Dependent Coproporphyrinogen Oxidase

1TKL の概要

• エントリーDOI: 10.2210/pdb1tkl/pdb
• 関連するPDBエントリー: 1TK1 1TLB
• 分子名称: Coproporphyrinogen III oxidase (2 entities in total)
• 機能のキーワード: coproporphyrinogen oxidase, heme biosynthesis, enzyme, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P11353
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75070.46

構造登録者

Phillips, J.D.,Whitby, F.G.,Warby, C.A.,Labbe, P.,Yang, C.,Pflugrath, J.W.,Ferrara, J.D.,Robinson, H.,Kushner, J.P.,Hill, C.P. (登録日: 2004-06-08, 公開日: 2004-07-20, 最終更新日: 2024-02-14)

主引用文献

Phillips, J.D.,Whitby, F.G.,Warby, C.A.,Labbe, P.,Yang, C.,Pflugrath, J.W.,Ferrara, J.D.,Robinson, H.,Kushner, J.P.,Hill, C.P.
Crystal Structure of the Oxygen-dependant Coproporphyrinogen Oxidase (Hem13p) of Saccharomyces cerevisiae
J.Biol.Chem., 279:38960-38968, 2004

PubMed Abstract: Coproporphyrinogen oxidase (CPO) is an essential enzyme that catalyzes the sixth step of the heme biosynthetic pathway. Unusually for heme biosynthetic enzymes, CPO exists in two evolutionarily and mechanistically distinct families, with eukaryotes and some prokaryotes employing members of the highly conserved oxygen-dependent CPO family. Here, we report the crystal structure of the oxygen-dependent CPO from Saccharomyces cerevisiae (Hem13p), which was determined by optimized sulfur anomalous scattering and refined to a resolution of 2.0 A. The protein adopts a novel structure that is quite different from predicted models and features a central flat seven-stranded anti-parallel sheet that is flanked by helices. The dimeric assembly, which is seen in different crystal forms, is formed by packing of helices and a short isolated strand that forms a beta-ladder with its counterpart in the partner subunit. The deep active-site cleft is lined by conserved residues and has been captured in open and closed conformations in two different crystal forms. A substratesized cavity is completely buried in the closed conformation by the approximately 8-A movement of a helix that forms a lid over the active site. The structure therefore suggests residues that likely play critical roles in catalysis and explains the deleterious effect of many of the mutations associated with the disease hereditary coproporphyria.

PubMed: 15194705
DOI: 10.1074/jbc.M406050200

実験手法

X-RAY DIFFRACTION (2 Å)