2ZAT

Crystal structure of a mammalian reductase

Summary for 2ZAT

• Entry DOI: 10.2210/pdb2zat/pdb
• Descriptor: Dehydrogenase/reductase SDR family member 4, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: alpha/beta, oxidoreductase
• Biological source: Sus scrofa (pig)
• Cellular location: Peroxisome: Q8WNV7
• Total number of polymer chains: 4
• Total formula weight: 114209.91

Authors

Tanaka, N.,Aoki, K.,Nakamura, K.T. (deposition date: 2007-10-10, release date: 2008-04-29, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)