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| ==Crystal Structure of Pseudomonas aeruginosa D-Arginine Dehydrogenase in Complex with an (N5) Flavin Adduct== | | ==Crystal Structure of Pseudomonas aeruginosa D-Arginine Dehydrogenase in Complex with an (N5) Flavin Adduct== |
- | <StructureSection load='3sm8' size='340' side='right' caption='[[3sm8]], [[Resolution|resolution]] 1.07Å' scene=''> | + | <StructureSection load='3sm8' size='340' side='right'caption='[[3sm8]], [[Resolution|resolution]] 1.07Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3sm8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SM8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SM8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sm8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SM8 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FNK:[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL+(2R,3S,4S)-5-[7,8-DIMETHYL-5-(3-METHYLBUTANOYL)-2,4-DIOXO-1,3,4,5-TETRAHYDROBENZO[G]PTERIDIN-10(2H)-YL]-2,3,4-TRIHYDROXYPENTYL+DIHYDROGEN+DIPHOSPHATE'>FNK</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.07Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nyc|3nyc]], [[3nye|3nye]], [[3nyf|3nyf]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FNK:[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl+(2R,3S,4S)-5-[7,8-dimethyl-5-(3-methylbutanoyl)-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl+dihydrogen+diphosphate'>FNK</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dauA, PA3863, PAO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</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=3sm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sm8 OCA], [https://pdbe.org/3sm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sm8 RCSB], [https://www.ebi.ac.uk/pdbsum/3sm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sm8 ProSAT]</span></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=3sm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sm8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sm8 RCSB], [http://www.ebi.ac.uk/pdbsum/3sm8 PDBsum]</span></td></tr> | + | |
| </table> | | </table> |
- | <div style="background-color:#fffaf0;">
| + | == Function == |
- | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/DAUA_PSEAE DAUA_PSEAE] DauA is highly expressed within the cystic fibrosis (CF) lung, and it is required for virulence via the optimal production of hydrogen cyanide, pyocyanine, pyoverdine, rhamnolipid and alginate during biofilm formation (PubMed:24011342). Involved in the catabolism of D-lysine and D-arginine. Under aerobic conditions, the arginine succinyltransferase (AST) and arginine transaminase (ATA) pathways are 2 major routes for L-arginine utilization as the sole source of carbon and nitrogen. The D-to-L racemization of arginine by DauA and DauB is necessary, before to be channeled into the AST and/or ATA pathways. DauA catalyzes the flavin-dependent oxidative deamination of D-arginine into 2-ketoarginine (2-KA) and ammonia (PubMed:3141581, PubMed:19139398, PubMed:19850617, PubMed:20809650). It has also dehydrogenase activity towards D-lysine, D-tyrosine, D-methionine, D-phenylalanine, D-ornithine, D-histidine and D-leucine as substrates (PubMed:19850617, PubMed:20809650).<ref>PMID:19139398</ref> <ref>PMID:19850617</ref> <ref>PMID:20809650</ref> <ref>PMID:24011342</ref> <ref>PMID:3141581</ref> |
- | d-Arginine dehydrogenase (DADH) catalyzes the flavin-dependent oxidative deamination of d-arginine and other d-amino acids to the corresponding imino acids. The 1.07 A atomic-resolution structure of DADH crystallized with d-leucine unexpectedly revealed a covalent N(5) flavin adduct, instead of the expected iminoleucine product in the active site. This acyl adduct has been successfully reproduced by photoreduction of DADH in the presence of 4-methyl-2-oxopentanoic acid (ketoleucine). The iminoleucine may be released readily because of weak interactions in the binding site, in contrast to iminoarginine, converted to ketoleucine, which reacts with activated FAD to form the covalently linked acyl adduct.
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- | | + | |
- | Atomic-Resolution Structure of an N(5) Flavin Adduct in d-Arginine Dehydrogenase.,Fu G, Yuan H, Wang S, Gadda G, Weber IT Biochemistry. 2011 Jul 26;50(29):6292-4. Epub 2011 Jul 5. PMID:21707047<ref>PMID:21707047</ref>
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- | | + | |
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
- | </div> | + | |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| + | [[Category: Large Structures]] |
| [[Category: Pseudomonas aeruginosa]] | | [[Category: Pseudomonas aeruginosa]] |
- | [[Category: Fu, G]] | + | [[Category: Fu G]] |
- | [[Category: Weber, I T]] | + | [[Category: Weber IT]] |
- | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
DAUA_PSEAE DauA is highly expressed within the cystic fibrosis (CF) lung, and it is required for virulence via the optimal production of hydrogen cyanide, pyocyanine, pyoverdine, rhamnolipid and alginate during biofilm formation (PubMed:24011342). Involved in the catabolism of D-lysine and D-arginine. Under aerobic conditions, the arginine succinyltransferase (AST) and arginine transaminase (ATA) pathways are 2 major routes for L-arginine utilization as the sole source of carbon and nitrogen. The D-to-L racemization of arginine by DauA and DauB is necessary, before to be channeled into the AST and/or ATA pathways. DauA catalyzes the flavin-dependent oxidative deamination of D-arginine into 2-ketoarginine (2-KA) and ammonia (PubMed:3141581, PubMed:19139398, PubMed:19850617, PubMed:20809650). It has also dehydrogenase activity towards D-lysine, D-tyrosine, D-methionine, D-phenylalanine, D-ornithine, D-histidine and D-leucine as substrates (PubMed:19850617, PubMed:20809650).[1] [2] [3] [4] [5]
References
- ↑ Li C, Lu CD. Arginine racemization by coupled catabolic and anabolic dehydrogenases. Proc Natl Acad Sci U S A. 2009 Jan 20;106(3):906-11. doi:, 10.1073/pnas.0808269106. Epub 2009 Jan 12. PMID:19139398 doi:http://dx.doi.org/10.1073/pnas.0808269106
- ↑ Li C, Yao X, Lu CD. Regulation of the dauBAR operon and characterization of D-amino acid dehydrogenase DauA in arginine and lysine catabolism of Pseudomonas aeruginosa PAO1. Microbiology (Reading). 2010 Jan;156(Pt 1):60-71. doi: 10.1099/mic.0.033282-0., Epub 2009 Oct 22. PMID:19850617 doi:http://dx.doi.org/10.1099/mic.0.033282-0
- ↑ Fu G, Yuan H, Li C, Lu CD, Gadda G, Weber IT. Conformational Changes and Substrate Recognition in Pseudomonas aeruginosa d-Arginine Dehydrogenase (,). Biochemistry. 2010 Sep 9. PMID:20809650 doi:10.1021/bi1005865
- ↑ Oliver KE, Silo-Suh L. Impact of D-amino acid dehydrogenase on virulence factor production by a Pseudomonas aeruginosa. Can J Microbiol. 2013 Sep;59(9):598-603. doi: 10.1139/cjm-2013-0289. Epub 2013, Jul 11. PMID:24011342 doi:http://dx.doi.org/10.1139/cjm-2013-0289
- ↑ Jann A, Matsumoto H, Haas D. The fourth arginine catabolic pathway of Pseudomonas aeruginosa. J Gen Microbiol. 1988 Apr;134(4):1043-53. doi: 10.1099/00221287-134-4-1043. PMID:3141581 doi:http://dx.doi.org/10.1099/00221287-134-4-1043
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