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| | <StructureSection load='5m42' size='340' side='right'caption='[[5m42]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5m42' size='340' side='right'caption='[[5m42]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m42]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M42 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M42 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M42 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C1214 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline_dehydrogenase Proline dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.5.2 1.5.5.2] </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=5m42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m42 OCA], [https://pdbe.org/5m42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m42 RCSB], [https://www.ebi.ac.uk/pdbsum/5m42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m42 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5m42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m42 OCA], [http://pdbe.org/5m42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m42 RCSB], [http://www.ebi.ac.uk/pdbsum/5m42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m42 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRODH_THET2 PRODH_THET2]] Converts proline to delta-1-pyrroline-5-carboxylate (PubMed:17344208, PubMed:18426222). Has significant activity against O(2) producing superoxide during proline oxidation catalytic cycle (PubMed:17344208).<ref>PMID:17344208</ref> <ref>PMID:18426222</ref> | + | [https://www.uniprot.org/uniprot/PRODH_THET2 PRODH_THET2] Converts proline to delta-1-pyrroline-5-carboxylate (PubMed:17344208, PubMed:18426222). Has significant activity against O(2) producing superoxide during proline oxidation catalytic cycle (PubMed:17344208).<ref>PMID:17344208</ref> <ref>PMID:18426222</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Proline dehydrogenase]] | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Thet2]]
| + | [[Category: Huijbers MME]] |
| - | [[Category: Berkel, W J.H van]]
| + | [[Category: Martinez-Julvez M]] |
| - | [[Category: Huijbers, M M.E]] | + | [[Category: Medina M]] |
| - | [[Category: Martinez-Julvez, M]] | + | [[Category: Van Berkel WJH]] |
| - | [[Category: Medina, M]] | + | |
| - | [[Category: Beta8-alpha8-barrel]] | + | |
| - | [[Category: Flavoenzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
PRODH_THET2 Converts proline to delta-1-pyrroline-5-carboxylate (PubMed:17344208, PubMed:18426222). Has significant activity against O(2) producing superoxide during proline oxidation catalytic cycle (PubMed:17344208).[1] [2]
Publication Abstract from PubMed
Flavoenzymes are versatile biocatalysts containing either FAD or FMN as cofactor. FAD often binds to a Rossmann fold, while FMN prefers a TIM-barrel or flavodoxin-like fold. Proline dehydrogenase is denoted as an exception: it possesses a TIM barrel-like fold while binding FAD. Using a riboflavin auxotrophic Escherichia coli strain and maltose-binding protein as solubility tag, we produced the apoprotein of Thermus thermophilus ProDH (MBP-TtProDH). Remarkably, reconstitution with FAD or FMN revealed that MBP-TtProDH has no preference for either of the two prosthetic groups. Kinetic parameters of both holo forms are similar, as are the dissociation constants for FAD and FMN release. Furthermore, we show that the holo form of MBP-TtProDH, as produced in E. coli TOP10 cells, contains about three times more FMN than FAD. In line with this flavin content, the crystal structure of TtProDH variant DeltaABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. To the best of our knowledge, this is the first example of a flavoenzyme that does not discriminate between FAD and FMN as cofactor. Therefore, classification of TtProDH as an FAD-binding enzyme should be reconsidered.
Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor.,Huijbers MM, Martinez-Julvez M, Westphal AH, Delgado-Arciniega E, Medina M, van Berkel WJ Sci Rep. 2017 Mar 3;7:43880. doi: 10.1038/srep43880. PMID:28256579[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ White TA, Krishnan N, Becker DF, Tanner JJ. Structure and kinetics of monofunctional proline dehydrogenase from Thermus thermophilus. J Biol Chem. 2007 May 11;282(19):14316-27. Epub 2007 Mar 7. PMID:17344208 doi:10.1074/jbc.M700912200
- ↑ White TA, Johnson WH Jr, Whitman CP, Tanner JJ. Structural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine. Biochemistry. 2008 May 20;47(20):5573-80. Epub 2008 Apr 22. PMID:18426222 doi:10.1021/bi800055w
- ↑ Huijbers MM, Martinez-Julvez M, Westphal AH, Delgado-Arciniega E, Medina M, van Berkel WJ. Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor. Sci Rep. 2017 Mar 3;7:43880. doi: 10.1038/srep43880. PMID:28256579 doi:http://dx.doi.org/10.1038/srep43880
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