2ZAT

Crystal structure of a mammalian reductase

2ZAT の概要

• エントリーDOI: 10.2210/pdb2zat/pdb
• 分子名称: Dehydrogenase/reductase SDR family member 4, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: alpha/beta, oxidoreductase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Peroxisome: Q8WNV7
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114209.91

構造登録者

Tanaka, N.,Aoki, K.,Nakamura, K.T. (登録日: 2007-10-10, 公開日: 2008-04-29, 最終更新日: 2023-11-01)

主引用文献

Tanaka, N.,Aoki, K.,Ishikura, S.,Nagano, M.,Imamura, Y.,Hara, A.,Nakamura, K.T.
Molecular basis for peroxisomal localization of tetrameric carbonyl reductase.
Structure, 16:388-397, 2008

PubMed Abstract: Pig heart peroxisomal carbonyl reductase (PerCR) belongs to the short-chain dehydrogenase/reductase family, and its sequence comprises a C-terminal SRL tripeptide, which is a variant of the type 1 peroxisomal targeting signal (PTS1) Ser-Lys-Leu. PerCR is imported into peroxisomes of HeLa cells when the cells are transfected with vectors expressing the enzyme. However, PerCR does not show specific targeting when introduced into the cells with a protein transfection reagent. To understand the structural basis for peroxisomal localization of PerCR, we determined the crystal structure of PerCR. Our data revealed that the C-terminal PTS1 of each subunit of PerCR was involved in intersubunit interactions and was buried in the interior of the tetrameric molecule. These findings indicate that the PTS1 receptor Pex5p in the cytosol recognizes the monomeric form of PerCR whose C-terminal PTS1 is exposed, and that this PerCR is targeted into the peroxisome, thereby forming a tetramer.

PubMed: 18334214
DOI: 10.1016/j.str.2007.12.022

実験手法

X-RAY DIFFRACTION (1.5 Å)