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1cyd

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Revision as of 04:13, 10 September 2015

CARBONYL REDUCTASE COMPLEXED WITH NADPH AND 2-PROPANOL

Structural highlights

1cyd is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Carbonyl reductase (NADPH), with EC number 1.1.1.184
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CBR2_MOUSE] May function in the pulmonary metabolism of endogenous carbonyl compounds, such as aliphatic aldehydes and ketones derived from lipid peroxidation, 3-ketosteroids and fatty aldehydes, as well as in xenobiotic metabolism.^[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

BACKGROUND: Mouse lung carbonyl reductase (MLCR) is a member of the short-chain dehydrogenase/reductase (SDR) family. Although it uses both NADPH and NADH as coenzymes, the structural basis of its strong preference for NADPH is unknown. RESULTS: The crystal structure of the ternary complex of MLCR (with NADPH and 2-propanol) has been determined at 1.8 A resolution. This is the first three-dimensional structure of a carbonyl reductase, and MLCR is the first member of the SDR family to be solved in complex with NADPH (rather than NADH). Comparison of the MLCR ternary complex with three structures reported previously for enzymes of the SDR family (all crystallized as complexes with NADH) reveals a pair of basic residues (Lys17 and Arg39) making strong electrostatic interactions with the 2'-phosphate group of NADPH. This pair of residues is well conserved among the NADPH-preferring enzymes of the SDR family, but not among the NADH-preferring enzymes. In the latter, an aspartate side chain occupies the position of the two basic side chains. The aspartate residue, which would come into unacceptably close contact with the 2'-phosphate group of the adenosine moiety of NADPH, is replaced by a threonine or alanine in the primary sequences of NADPH-preferring enzymes of the SDR family. CONCLUSIONS: The cofactor preferences exhibited by the enzymes of the SDR family are mainly determined by the electrostatic environment surrounding the 2'-hydroxyl (or phosphate) group of the adenosine ribose moiety of NADH (or NADPH). Thus, positively charged and negatively charged environments correlate with preference for NADPH and NADH respectively.

Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family.,Tanaka N, Nonaka T, Nakanishi M, Deyashiki Y, Hara A, Mitsui Y Structure. 1996 Jan 15;4(1):33-45. PMID:8805511^[2]

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

References

↑ Nakanishi M, Deyashiki Y, Ohshima K, Hara A. Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase. Identity with an adipocyte 27-kDa protein. Eur J Biochem. 1995 Mar 1;228(2):381-7. PMID:7705352
↑ Tanaka N, Nonaka T, Nakanishi M, Deyashiki Y, Hara A, Mitsui Y. Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure. 1996 Jan 15;4(1):33-45. PMID:8805511

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonyl_reductase_(NADPH) Carbonyl reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.184 1.1.1.184] </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=1cyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cyd RCSB], [http://www.ebi.ac.uk/pdbsum/1cyd 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=1cyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyd OCA], [http://pdbe.org/1cyd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cyd RCSB], [http://www.ebi.ac.uk/pdbsum/1cyd PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1cyd" style="background-color:#fffaf0;"></div>
 ==See Also==

1cyd

From Proteopedia

Revision as of 04:13, 10 September 2015

CARBONYL REDUCTASE COMPLEXED WITH NADPH AND 2-PROPANOL

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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