Crystal Structure of Pseudomonas aeruginosa D-Arginine DehydrogenaseCrystal Structure of Pseudomonas aeruginosa D-Arginine Dehydrogenase

Structural highlights

3nyc is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.06Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. 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
  2. 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
  3. 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
  4. 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
  5. 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

3nyc, resolution 1.06Å

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