1N5D

CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE

Replaces:  1HU4

Summary for 1N5D

• Entry DOI: 10.2210/pdb1n5d/pdb
• Descriptor: CARBONYL REDUCTASE/20BETA-HYDROXYSTEROID DEHYDROGENASE, SULFATE ION, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: shortchain dehydrogenase/reductase, monomer, nadp-complex, oxidoreductase
• Biological source: Sus scrofa (pig)
• Cellular location: Cytoplasm : Q28960
• Total number of polymer chains: 1
• Total formula weight: 32441.56

Authors

Ghosh, D. (deposition date: 2002-11-05, release date: 2002-11-13, Last modification date: 2024-02-14)

Primary citation

Ghosh, D.,Sawicki, M.,Pletnev, V.,Erman, M.,Duax, W.L.,Ohno, S.,Nakajin, S.
Porcine Carbonyl Reductase: Structural Basis for a Functional Monomer in Short-Chain Dehydrogenases/Reductases
J.Biol.Chem., 276:18457-18463, 2001

PubMed Abstract: Porcine testicular carbonyl reductase (PTCR) belongs to the short chain dehydrogenases/reductases (SDR) superfamily and catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. The enzyme shares nearly 85% sequence identity with the NADPH-dependent human 15-hydroxyprostaglandin dehydrogenase/carbonyl reductase. The tertiary structure of the enzyme at 2.3 A reveals a fold characteristic of the SDR superfamily that uses a Tyr-Lys-Ser triad as catalytic residues, but exhibits neither the functional homotetramer nor the homodimer that distinguish all SDRs. It is the first known monomeric structure in the SDR superfamily. In PTCR, which is also active as a monomer, a 41-residue insertion immediately before the catalytic Tyr describes an all-helix subdomain that packs against interfacial helices, eliminating the four-helix bundle interface conserved in the superfamily. An additional anti-parallel strand in the PTCR structure also blocks the other strand-mediated interface. These novel structural features provide the basis for the scaffolding of one catalytic site within a single molecule of the enzyme.

PubMed: 11279087
DOI: 10.1074/jbc.M100538200

Experimental method

X-RAY DIFFRACTION (2.3 Å)