1n5d
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(New page: 200px<br /><applet load="1n5d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n5d, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 19:51, 20 November 2007
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CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE
Overview
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.
About this Structure
1N5D is a Single protein structure of sequence from Sus scrofa with SO4 and NDP as ligands. This structure superseeds the now removed PDB entry 1HU4. Active as 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase, with EC number 1.1.1.53 Full crystallographic information is available from OCA.
Reference
Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases., Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL, J Biol Chem. 2001 May 25;276(21):18457-63. Epub 2001 Mar 8. PMID:11279087
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