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1n5d

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Revision as of 14:45, 12 October 2017

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

Structural highlights

1n5d is a 1 chain structure with sequence from Pig. This structure supersedes the now removed PDB entry 1hu4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase, with EC number 1.1.1.53
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CBR1_PIG] NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (By similarity).^[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

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.

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^[2]

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

References

↑ Tanaka M, Ohno S, Adachi S, Nakajin S, Shinoda M, Nagahama Y. Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase. J Biol Chem. 1992 Jul 5;267(19):13451-5. PMID:1377683
↑ Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL. Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases. J Biol Chem. 2001 May 25;276(21):18457-63. Epub 2001 Mar 8. PMID:11279087 doi:10.1074/jbc.M100538200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n5d"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE==
 <StructureSection load='1n5d' size='340' side='right' caption='[[1n5d]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hu4 1hu4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N5D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hu4 1hu4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N5D FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-alpha-(or_20-beta)-hydroxysteroid_dehydrogenase 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.53 1.1.1.53] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n5d OCA], [http://pdbe.org/1n5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n5d RCSB], [http://www.ebi.ac.uk/pdbsum/1n5d PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n5d OCA], [http://pdbe.org/1n5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n5d RCSB], [http://www.ebi.ac.uk/pdbsum/1n5d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n5d ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1n5d" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Hydroxysteroid dehydrogenase|Hydroxysteroid dehydrogenase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Sus scrofa]]
+[[Category: Pig]]
 [[Category: Ghosh, D]]
 [[Category: Monomer]]

1n5d

From Proteopedia

Revision as of 14:45, 12 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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