|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3vxg' size='340' side='right'caption='[[3vxg]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3vxg' size='340' side='right'caption='[[3vxg]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vxg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_22019 Atcc 22019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VXG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vxg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_parapsilosis Candida parapsilosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VXG FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4h8n|4h8n]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cpr-c2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5480 ATCC 22019])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/2-dehydropantolactone_reductase_((Si)-specific) 2-dehydropantolactone reductase ((Si)-specific)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.214 1.1.1.214] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vxg OCA], [https://pdbe.org/3vxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vxg RCSB], [https://www.ebi.ac.uk/pdbsum/3vxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vxg ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vxg OCA], [https://pdbe.org/3vxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vxg RCSB], [https://www.ebi.ac.uk/pdbsum/3vxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vxg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CPRC2_CANPA CPRC2_CANPA] NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. Reduces ketopantoyl lactone and isatin. Does not act on menadione, p-nitrobenzaldehyde and pyridine-3-aldehyde.<ref>PMID:11826979</ref> <ref>PMID:14593510</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 22019]] | + | [[Category: Candida parapsilosis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kataoka, M]] | + | [[Category: Kataoka M]] |
| - | [[Category: Maruoka, S]] | + | [[Category: Maruoka S]] |
| - | [[Category: Miyakawa, T]] | + | [[Category: Miyakawa T]] |
| - | [[Category: Nagata, K]] | + | [[Category: Nagata K]] |
| - | [[Category: Ohtsuka, J]] | + | [[Category: Ohtsuka J]] |
| - | [[Category: Qin, H M]] | + | [[Category: Qin H-M]] |
| - | [[Category: Shimizu, S]] | + | [[Category: Shimizu S]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Tanokura M]] |
| - | [[Category: Yamamura, A]] | + | [[Category: Yamamura A]] |
| - | [[Category: D-pantoyl lactone]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
CPRC2_CANPA NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. Reduces ketopantoyl lactone and isatin. Does not act on menadione, p-nitrobenzaldehyde and pyridine-3-aldehyde.[1] [2]
Publication Abstract from PubMed
Conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708, identified as a nicotinamide adenine dinucleotide phosphate (NADPH)-dependent ketopantoyl lactone reductase, belongs to the aldo-keto reductase superfamily. This enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner. To elucidate the structural basis of the substrate specificity, we determined the crystal structures of the apo CPR-C2 and CPR-C2/NADPH complex at 1.70 and 1.80 A resolutions, respectively. CPR-C2 adopted a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induced conformational changes in which Thr27 and Lys28 moved 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds. Based on the comparison of the CPR-C2/NADPH structure with 3-alpha-hydroxysteroid dehydrogenase and mutation analyses, we constructed substrate binding models with ketopantoyl lactone, which provided insight into the substrate specificity by the cofactor-induced structure. The results will be useful for the rational design of CPR-C2 mutants targeted for use in the industrial manufacture of ketopantoyl lactone.
Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding.,Qin HM, Yamamura A, Miyakawa T, Kataoka M, Nagai T, Kitamura N, Urano N, Maruoka S, Ohtsuka J, Nagata K, Shimizu S, Tanokura M Appl Microbiol Biotechnol. 2013 Jul 5. PMID:23828603[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hidalgo AR, Akond MA, Kita K, Kataoka M, Shimizu S. Isolation and primary structural analysis of two conjugated polyketone reductases from Candida parapsilosis. Biosci Biotechnol Biochem. 2001 Dec;65(12):2785-8. doi: 10.1271/bbb.65.2785. PMID:11826979 doi:http://dx.doi.org/10.1271/bbb.65.2785
- ↑ Kataoka M, Delacruz-Hidalgo AR, Akond MA, Sakuradani E, Kita K, Shimizu S. Gene cloning and overexpression of two conjugated polyketone reductases, novel aldo-keto reductase family enzymes, of Candida parapsilosis. Appl Microbiol Biotechnol. 2004 Apr;64(3):359-66. doi: 10.1007/s00253-003-1484-3., Epub 2003 Oct 31. PMID:14593510 doi:http://dx.doi.org/10.1007/s00253-003-1484-3
- ↑ Qin HM, Yamamura A, Miyakawa T, Kataoka M, Nagai T, Kitamura N, Urano N, Maruoka S, Ohtsuka J, Nagata K, Shimizu S, Tanokura M. Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding. Appl Microbiol Biotechnol. 2013 Jul 5. PMID:23828603 doi:10.1007/s00253-013-5073-9
|
