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| | <StructureSection load='2fss' size='340' side='right'caption='[[2fss]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2fss' size='340' side='right'caption='[[2fss]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fss]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18810 Atcc 18810]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FSS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fss]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_boidinii Candida boidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FSS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2a1z|2a1z]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cbfdh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5477 ATCC 18810])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2] </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=2fss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fss OCA], [https://pdbe.org/2fss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fss RCSB], [https://www.ebi.ac.uk/pdbsum/2fss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fss 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=2fss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fss OCA], [https://pdbe.org/2fss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fss RCSB], [https://www.ebi.ac.uk/pdbsum/2fss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fss ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FDH_CANBO FDH_CANBO] Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.[HAMAP-Rule:MF_03210]<ref>PMID:1248477</ref> <ref>PMID:9226256</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18810]] | |
| - | [[Category: Formate dehydrogenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lamzin, V S]] | + | [[Category: Lamzin VS]] |
| - | [[Category: Schirwitz, K]] | + | [[Category: Schirwitz K]] |
| - | [[Category: Schmidt, A]] | + | [[Category: Schmidt A]] |
| - | [[Category: Formate binding site]]
| + | |
| - | [[Category: Nad binding site]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Protein homo dimer]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
FDH_CANBO Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.[HAMAP-Rule:MF_03210][1] [2]
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
The understanding of the mechanism of enzymatic recovery of NADH is of biological and of considerable biotechnological interest, since the essential, but expensive, cofactor NADH is exhausted in asymmetric hydrogenation processes, but can be recovered by NAD(+)-dependent formate dehydrogenase (FDH). Most accepted for this purpose is the FDH from the yeast Candida boidinii (CbFDH), which, having relatively low thermostability and specific activity, has been targeted by enzyme engineering for several years. Optimization by mutagenesis studies was performed based on physiological studies and structure modeling. However, X-ray structural information has been required in order to clarify the enzymatic mechanism and to enhance the effectiveness and operational stability of enzymatic cofactor regenerators in biocatalytic enantiomer synthesis as well as to explain the observed biochemical differences between yeast and bacterial FDH. We designed two single-point mutants in CbFDH using an adapted surface engineering approach, and this allowed crystals suitable for high-resolution X-ray structural studies to be obtained. The mutations improved the crystallizability of the protein and also the catalytic properties and the stability of the enzyme. With these crystal structures, we explain the observed differences from both sources, and form the basis for further rational mutagenesis studies.
High-resolution structures of formate dehydrogenase from Candida boidinii.,Schirwitz K, Schmidt A, Lamzin VS Protein Sci. 2007 Jun;16(6):1146-56. PMID:17525463[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schüte H, Flossdorf J, Sahm H, Kula MR. Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii. Eur J Biochem. 1976 Feb 2;62(1):151-60. PMID:1248477 doi:10.1111/j.1432-1033.1976.tb10108.x
- ↑ Sakai Y, Murdanoto AP, Konishi T, Iwamatsu A, Kato N. Regulation of the formate dehydrogenase gene, FDH1, in the methylotrophic yeast Candida boidinii and growth characteristics of an FDH1-disrupted strain on methanol, methylamine, and choline. J Bacteriol. 1997 Jul;179(14):4480-5. PMID:9226256 doi:10.1128/jb.179.14.4480-4485.1997
- ↑ Schirwitz K, Schmidt A, Lamzin VS. High-resolution structures of formate dehydrogenase from Candida boidinii. Protein Sci. 2007 Jun;16(6):1146-56. PMID:17525463 doi:16/6/1146
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