2zat

From Proteopedia

Crystal structure of a mammalian reductase

PDB ID 2zat

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Structural highlights

2zat is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DHRS4_PIG Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Molecular basis for peroxisomal localization of tetrameric carbonyl reductase.,Tanaka N, Aoki K, Ishikura S, Nagano M, Imamura Y, Hara A, Nakamura KT Structure. 2008 Mar;16(3):388-97. PMID:18334214^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Usami N, Ishikura S, Abe H, Nagano M, Uebuchi M, Kuniyasu A, Otagiri M, Nakayama H, Imamura Y, Hara A. Cloning, expression and tissue distribution of a tetrameric form of pig carbonyl reductase. Chem Biol Interact. 2003 Feb 1;143-144:353-61. PMID:12604222
↑ Tanaka N, Aoki K, Ishikura S, Nagano M, Imamura Y, Hara A, Nakamura KT. Molecular basis for peroxisomal localization of tetrameric carbonyl reductase. Structure. 2008 Mar;16(3):388-97. PMID:18334214 doi:10.1016/j.str.2007.12.022