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| | ==Crystal structure of the periplasmic pyoverdine maturation protein PvdP== | | ==Crystal structure of the periplasmic pyoverdine maturation protein PvdP== |
| - | <StructureSection load='6eys' size='340' side='right' caption='[[6eys]], [[Resolution|resolution]] 2.09Å' scene=''> | + | <StructureSection load='6eys' size='340' side='right'caption='[[6eys]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6eys]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseab Pseab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EYS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6eys]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_UCBPP-PA14 Pseudomonas aeruginosa UCBPP-PA14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EYS FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pvdP, PA14_33740 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208963 PSEAB])</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]] 2.091Å</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=6eys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eys OCA], [http://pdbe.org/6eys PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eys RCSB], [http://www.ebi.ac.uk/pdbsum/6eys PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eys 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=6eys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eys OCA], [https://pdbe.org/6eys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eys RCSB], [https://www.ebi.ac.uk/pdbsum/6eys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eys ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H2ZBG1_PSEAB A0A0H2ZBG1_PSEAB] |
| | <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: Pseab]] | + | [[Category: Large Structures]] |
| - | [[Category: Blankenfeldt, W]] | + | [[Category: Pseudomonas aeruginosa UCBPP-PA14]] |
| - | [[Category: Poppe, J]] | + | [[Category: Blankenfeldt W]] |
| - | [[Category: Barrel]] | + | [[Category: Poppe J]] |
| - | [[Category: Multidomain]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Pyoverdine]]
| + | |
| - | [[Category: Tyrosinase]]
| + | |
| Structural highlights
Function
A0A0H2ZBG1_PSEAB
Publication Abstract from PubMed
Pyoverdines (PVDs) are important chromophore-containing siderophores of fluorescent pseudomonad bacteria such as the opportunistic human pathogen Pseudomonas aeruginosa, in which they play an essential role in host infection. PVD biosynthesis encompasses a complex pathway comprising cytosolic non-ribosomal peptide synthetases which produce a polypeptide precursor that periplasmic enzymes convert to the final product. The structures of most enzymes involved in PVD chromophore maturation have been elucidated, but the structure of the essential tyrosinase PvdP, a monooxygenase required for the penultimate step in PVD biosynthesis, is not known. Here, we closed this gap by determining the crystal structure of PvdP in an apo- and tyrosine-complexed state at 2.1 and 2.7 A, respectively. These structures revealed that PvdP is a homodimer, with each chain consisting of a C-terminal tyrosinase domain and an N-terminal eight-stranded beta-barrel reminiscent of streptavidin that appears to have a structural role only. We observed that ligand binding leads to the displacement of a "placeholder" tyrosine that blocks the active site in the apo structure. This exposes a large, deep binding site that seems suitable for accommodating ferribactin, a substrate of PvdP in PVD biosynthesis. The binding site consists almost exclusively of residues from the tyrosinase domain. Of note, we also found that this domain is more closely related to tyrosinases from arthropods rather than to tyrosinases from other bacteria. In conclusion, our work unravels the structural basis of PvdP's activity in PVD biosynthesis, observations that may inform structure-guided development of PvdP-specific inhibitors to manage P. aeruginosa infections.
Pseudomonas aeruginosa pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinases.,Poppe J, Reichelt J, Blankenfeldt W J Biol Chem. 2018 Jul 20. pii: RA118.002560. doi: 10.1074/jbc.RA118.002560. PMID:30030378[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Poppe J, Reichelt J, Blankenfeldt W. Pseudomonas aeruginosa pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinases. J Biol Chem. 2018 Jul 20. pii: RA118.002560. doi: 10.1074/jbc.RA118.002560. PMID:30030378 doi:http://dx.doi.org/10.1074/jbc.RA118.002560
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