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| | <StructureSection load='4urp' size='340' side='right'caption='[[4urp]], [[Resolution|resolution]] 2.99Å' scene=''> | | <StructureSection load='4urp' size='340' side='right'caption='[[4urp]], [[Resolution|resolution]] 2.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4urp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4URP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4urp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4URP FirstGlance]. <br> |
| - | </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=4urp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urp OCA], [http://pdbe.org/4urp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4urp RCSB], [http://www.ebi.ac.uk/pdbsum/4urp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4urp ProSAT]</span></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]] 2.991Å</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=4urp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urp OCA], [https://pdbe.org/4urp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4urp RCSB], [https://www.ebi.ac.uk/pdbsum/4urp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4urp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FRM2_YEAST FRM2_YEAST]] Involved in negative regulation of fatty acid metabolism.<ref>PMID:8701605</ref> | + | [https://www.uniprot.org/uniprot/FRM2_YEAST FRM2_YEAST] Involved in negative regulation of fatty acid metabolism.<ref>PMID:8701605</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bang, S Y]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Jung, D G]] | + | [[Category: Bang S-Y]] |
| - | [[Category: Park, S G]] | + | [[Category: Jung D-G]] |
| - | [[Category: Song, H N]] | + | [[Category: Park S-G]] |
| - | [[Category: Woo, E J]] | + | [[Category: Song H-N]] |
| - | [[Category: Nitrocompound]]
| + | [[Category: Woo E-J]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
FRM2_YEAST Involved in negative regulation of fatty acid metabolism.[1]
Publication Abstract from PubMed
Nitroreductases are flavoenzymes that catalyze nitrocompounds and are widely utilized in industrial applications due to their detoxification potential and activation of bio-medicinal pro-drugs. Type I nitroreductases are classified into subgroups depending on the use of NADPH or NADH as the electron donor. Here, we report the crystal structure of the fungal nitroreductase Frm2 from Saccharomyces cerevisiae, one of the uncharacterized subgroups of proteins, to reveal its minimal architecture previously observed in bacterial nitroreductases such as CinD and YdjA. The structure lacks protruding helical motifs that form part of the cofactor and substrate binding site, resulting in an open and wide active site geometry. Arg82 is uniquely conserved in proximity to the substrate binding site in Frm2 homologues and plays a crucial role in the activity of the active site. Frm2 primarily utilizes NADH to reduce 4-NQO. Because missing helical elements are involved in the direct binding to the NAD(P)H in group A or group B in Type I family, Frm2 and its homologues may represent a distinctive subgroup with an altered binding mode for the reducing compound. This result provides a structural basis for the rational design of novel pro-drugs with the ability to reduce nitrogen-containing hazardous molecules. This article is protected by copyright. All rights reserved.
Crystal structure of the fungal nitroreductase Frm2 from Saccharomyces cerevisiae.,Song HN, Jeong DG, Bang SY, Paek SH, Park BC, Park SG, Woo EJ Protein Sci. 2015 Apr 11. doi: 10.1002/pro.2686. PMID:25864423[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McHale MW, Kroening KD, Bernlohr DA. Identification of a class of Saccharomyces cerevisiae mutants defective in fatty acid repression of gene transcription and analysis of the frm2 gene. Yeast. 1996 Mar 30;12(4):319-31. PMID:8701605 doi:<319::AID-YEA914>3.0.CO;2-# http://dx.doi.org/10.1002/(SICI)1097-0061(19960330)12:4<319::AID-YEA914>3.0.CO;2-#
- ↑ Song HN, Jeong DG, Bang SY, Paek SH, Park BC, Park SG, Woo EJ. Crystal structure of the fungal nitroreductase Frm2 from Saccharomyces cerevisiae. Protein Sci. 2015 Apr 11. doi: 10.1002/pro.2686. PMID:25864423 doi:http://dx.doi.org/10.1002/pro.2686
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