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| | ==Ornithine Hydroxylase (PvdA) from Pseudomonas aeruginosa== | | ==Ornithine Hydroxylase (PvdA) from Pseudomonas aeruginosa== |
| - | <StructureSection load='3s5w' size='340' side='right' caption='[[3s5w]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3s5w' size='340' side='right'caption='[[3s5w]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3s5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S5W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3s5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S5W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ONH:N~5~-HYDROXY-L-ORNITHINE'>ONH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ONH:N~5~-HYDROXY-L-ORNITHINE'>ONH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s61|3s61]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s61|3s61]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA2386, pvd-1, pvdA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA2386, pvd-1, pvdA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=3s5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s5w OCA], [http://pdbe.org/3s5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s5w RCSB], [http://www.ebi.ac.uk/pdbsum/3s5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s5w 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=3s5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s5w OCA], [https://pdbe.org/3s5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s5w RCSB], [https://www.ebi.ac.uk/pdbsum/3s5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s5w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PVDA_PSEAE PVDA_PSEAE]] Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as pyoverdin. Pyoverdin is a hydroxamate siderophore composed of a 6,7-dihydroxyquinoline-containing fluorescent chromophore joined to the N-terminus of a partly cyclic octapeptide (D-Ser-L-Arg-D-Ser-L-N(5)-OH-Orn-L-Lys-L-N(5)-OH-Orn-L-Thr-L-Thr in strain PAO1). Specific for NADPH, which plays a role in stabilization of the C4a-hydroperoxyflavin intermediate.<ref>PMID:17015659</ref> <ref>PMID:19368334</ref> <ref>PMID:8106324</ref> | + | [[https://www.uniprot.org/uniprot/PVDA_PSEAE PVDA_PSEAE]] Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as pyoverdin. Pyoverdin is a hydroxamate siderophore composed of a 6,7-dihydroxyquinoline-containing fluorescent chromophore joined to the N-terminus of a partly cyclic octapeptide (D-Ser-L-Arg-D-Ser-L-N(5)-OH-Orn-L-Lys-L-N(5)-OH-Orn-L-Thr-L-Thr in strain PAO1). Specific for NADPH, which plays a role in stabilization of the C4a-hydroperoxyflavin intermediate.<ref>PMID:17015659</ref> <ref>PMID:19368334</ref> <ref>PMID:8106324</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Lamb, A L]] | | [[Category: Lamb, A L]] |
| | [[Category: Olucha, J]] | | [[Category: Olucha, J]] |
| Structural highlights
3s5w is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , |
| Related: | |
| Gene: | PA2386, pvd-1, pvdA ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[PVDA_PSEAE] Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as pyoverdin. Pyoverdin is a hydroxamate siderophore composed of a 6,7-dihydroxyquinoline-containing fluorescent chromophore joined to the N-terminus of a partly cyclic octapeptide (D-Ser-L-Arg-D-Ser-L-N(5)-OH-Orn-L-Lys-L-N(5)-OH-Orn-L-Thr-L-Thr in strain PAO1). Specific for NADPH, which plays a role in stabilization of the C4a-hydroperoxyflavin intermediate.[1] [2] [3]
Publication Abstract from PubMed
The ornithine hydroxylase from Pseudomonas aeruginosa (PvdA) catalyzes the FAD dependent hydroxylation of the sidechain amine of ornithine, which is subsequently formylated to generate the iron chelating hydroxamates of the siderophore pyoverdin. PvdA belongs to the class B flavoprotein monooxygenases, which catalyze the oxidation of substrates using NADPH as electron donor and molecular oxygen. Class B enzymes include the well-studied flavin-containing monooxygenases and Baeyer-Villiger monoogenases. The first two structures of a class B N-hydroxylating monooxygenase were determined with the FAD in oxidized (1.9 A resolution) and reduced states (3.03 A). PvdA has the two expected Rossman-like dinucleotide binding domains for FAD and NADPH, and also a substrate binding domain, with the active site at the interface between the three domains. The structures have NADP(H) and (hydroxy)ornithine bound in a solvent exposed active site, providing structural evidence for substrate and co-substrate specificity and the inability of PvdA to bind FAD tightly. Structural and biochemical evidence indicate that NADP+ remains bound throughout the oxidative half-reaction, which is proposed to shelter the flavin intermediates from solvent and thereby prevent uncoupling of NADPH oxidation from hydroxylated product formation.
Two structures of an N-hydroxylating flavoprotein monooxgenase: the ornithine hydroxylase from Pseudomonas aeruginosa.,Olucha J, Meneely KM, Chilton AS, Lamb AL J Biol Chem. 2011 Jul 13. PMID:21757711[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ge L, Seah SY. Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. J Bacteriol. 2006 Oct;188(20):7205-10. PMID:17015659 doi:http://dx.doi.org/10.1128/JB.00949-06
- ↑ Meneely KM, Barr EW, Bollinger JM Jr, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 2009 May 26;48(20):4371-6. doi: 10.1021/bi900442z. PMID:19368334 doi:http://dx.doi.org/10.1021/bi900442z
- ↑ Visca P, Ciervo A, Orsi N. Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa. J Bacteriol. 1994 Feb;176(4):1128-40. PMID:8106324
- ↑ Olucha J, Meneely KM, Chilton AS, Lamb AL. Two structures of an N-hydroxylating flavoprotein monooxgenase: the ornithine hydroxylase from Pseudomonas aeruginosa. J Biol Chem. 2011 Jul 13. PMID:21757711 doi:10.1074/jbc.M111.265876
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