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| | ==F420-dependent glucose-6-phosphate dehydrogenase from Rhodococcus jostii RHA1== | | ==F420-dependent glucose-6-phosphate dehydrogenase from Rhodococcus jostii RHA1== |
| - | <StructureSection load='5lxe' size='340' side='right' caption='[[5lxe]], [[Resolution|resolution]] 1.47Å' scene=''> | + | <StructureSection load='5lxe' size='340' side='right'caption='[[5lxe]], [[Resolution|resolution]] 1.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lxe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LXE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lxe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_jostii_RHA1 Rhodococcus jostii RHA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LXE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.47Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase_(coenzyme-F420) Glucose-6-phosphate dehydrogenase (coenzyme-F420)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.98.2 1.1.98.2] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5lxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lxe OCA], [http://pdbe.org/5lxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lxe RCSB], [http://www.ebi.ac.uk/pdbsum/5lxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lxe 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=5lxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lxe OCA], [https://pdbe.org/5lxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lxe RCSB], [https://www.ebi.ac.uk/pdbsum/5lxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lxe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FGD1_RHOJR FGD1_RHOJR]] Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. | + | [https://www.uniprot.org/uniprot/FGD1_RHOJR FGD1_RHOJR] Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5lxe" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5lxe" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Binda, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Fraaije, M W]] | + | [[Category: Rhodococcus jostii RHA1]] |
| - | [[Category: Mattevi, A]] | + | [[Category: Binda C]] |
| - | [[Category: Nguyen, Q-.T]] | + | [[Category: Fraaije MW]] |
| - | [[Category: Trinco, G]] | + | [[Category: Mattevi A]] |
| - | [[Category: Bacterial luciferase family]] | + | [[Category: Nguyen Q-T]] |
| - | [[Category: F420]]
| + | [[Category: Trinco G]] |
| - | [[Category: Glucose-6-phosphate dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]] | + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
FGD1_RHOJR Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone.
Publication Abstract from PubMed
Cofactor F420, a 5-deazaflavin involved in obligatory hydride transfer, is widely distributed among archaeal methanogens and actinomycetes. Owing to the low redox potential of the cofactor, F420-dependent enzymes play a pivotal role in central catabolic pathways and xenobiotic degradation processes in these organisms. A physiologically essential deazaflavoenzyme is the F420-dependent glucose-6-phosphate dehydrogenase (FGD), which catalyzes the reaction F420 + glucose-6-phosphate --> F420H2 + 6-phospho-gluconolactone. Thereby, FGDs generate the reduced F420 cofactor required for numerous F420H2-dependent reductases, involved e.g., in the bioreductive activation of the antitubercular prodrugs pretomanid and delamanid. We report here the identification, production, and characterization of three FGDs from Rhodococcus jostii RHA1 (Rh-FGDs), being the first experimental evidence of F420-dependent enzymes in this bacterium. The crystal structure of Rh-FGD1 has also been determined at 1.5 A resolution, showing a high similarity with FGD from Mycobacterium tuberculosis (Mtb) (Mtb-FGD1). The cofactor-binding pocket and active-site catalytic residues are largely conserved in Rh-FGD1 compared with Mtb-FGD1, except for an extremely flexible insertion region capping the active site at the C-terminal end of the TIM-barrel, which also markedly differs from other structurally related proteins. The role of the three positively charged residues (Lys197, Lys258, and Arg282) constituting the binding site of the substrate phosphate moiety was experimentally corroborated by means of mutagenesis study. The biochemical and structural data presented here provide the first step towards tailoring Rh-FGD1 into a more economical biocatalyst, e.g., an F420-dependent glucose dehydrogenase that requires a cheaper cosubstrate and can better match the demands for the growing applications of F420H2-dependent reductases in industry and bioremediation.
Discovery and characterization of an F420-dependent glucose-6-phosphate dehydrogenase (Rh-FGD1) from Rhodococcus jostii RHA1.,Nguyen QT, Trinco G, Binda C, Mattevi A, Fraaije MW Appl Microbiol Biotechnol. 2016 Dec 13. PMID:27966048[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nguyen QT, Trinco G, Binda C, Mattevi A, Fraaije MW. Discovery and characterization of an F420-dependent glucose-6-phosphate dehydrogenase (Rh-FGD1) from Rhodococcus jostii RHA1. Appl Microbiol Biotechnol. 2016 Dec 13. PMID:27966048 doi:http://dx.doi.org/10.1007/s00253-016-8038-y
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