5o8r: Difference between revisions
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==The crystal structure of DfoA bound to FAD and NADP; the desferrioxamine biosynthetic pathway cadaverine monooxygenase from the fire blight disease pathogen Erwinia amylovora== | ==The crystal structure of DfoA bound to FAD and NADP; the desferrioxamine biosynthetic pathway cadaverine monooxygenase from the fire blight disease pathogen Erwinia amylovora== | ||
<StructureSection load='5o8r' size='340' side='right' caption='[[5o8r]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='5o8r' size='340' side='right'caption='[[5o8r]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o8r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O8R OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5o8r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erwinia_amylovora_CFBP1430 Erwinia amylovora CFBP1430]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O8R FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id=' | <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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5o8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o8r OCA], [https://pdbe.org/5o8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o8r RCSB], [https://www.ebi.ac.uk/pdbsum/5o8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o8r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D4I246_ERWAC D4I246_ERWAC] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5o8r" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5o8r" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bartho | [[Category: Erwinia amylovora CFBP1430]] | ||
[[Category: Bellini | [[Category: Large Structures]] | ||
[[Category: Benini | [[Category: Bartho JD]] | ||
[[Category: Demitri | [[Category: Bellini D]] | ||
[[Category: Polsinelli | [[Category: Benini S]] | ||
[[Category: Salomone-Stagni | [[Category: Demitri N]] | ||
[[Category: Walsh | [[Category: Polsinelli I]] | ||
[[Category: Salomone-Stagni M]] | |||
[[Category: Walsh MA]] | |||
Latest revision as of 12:37, 6 December 2023
The crystal structure of DfoA bound to FAD and NADP; the desferrioxamine biosynthetic pathway cadaverine monooxygenase from the fire blight disease pathogen Erwinia amylovoraThe crystal structure of DfoA bound to FAD and NADP; the desferrioxamine biosynthetic pathway cadaverine monooxygenase from the fire blight disease pathogen Erwinia amylovora
Structural highlights
FunctionPublication Abstract from PubMedThe Gram-negative bacterium Erwinia amylovora is the etiological agent of fire blight, a devastating disease which affects Rosaceae such as apple, pear and quince. The siderophore desferrioxamine E plays an important role in bacterial pathogenesis by scavenging iron from the host. DfoJ, DfoA and DfoC are the enzymes responsible for desferrioxamine production starting from lysine. We have determined the crystal structures of each enzyme in the desferrioxamine E pathway and demonstrate that the biosynthesis involves the concerted action of DfoJ, followed by DfoA and lastly DfoC. These data provide the first crystal structures of a Group II pyridoxal-dependent lysine decarboxylase, a cadaverine monooxygenase and a desferrioxamine synthetase. DfoJ is a homodimer made up of three domains. Each monomer contributes to the completion of the active site, which is positioned at the dimer interface. DfoA is the first structure of a cadaverine monooxygenase. It forms homotetramers whose subunits are built by two domains: one for FAD and one for NADP(+) binding, the latter of which is formed by two subdomains. We propose a model for substrate binding and the role of residues 43-47 as gate keepers for FAD binding and the role of Arg97 in cofactors turnover. DfoC is the first structure of a desferrioxamine synthetase and the first of a multi-enzyme siderophore synthetase coupling an acyltransferase domain with a Non-Ribosomal Peptide Synthetase (NRPS)-Independent Siderophore domain (NIS). A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora.,Salomone-Stagni M, Bartho JD, Polsinelli I, Bellini D, Walsh MA, Demitri N, Benini S J Struct Biol. 2018 Feb 8. pii: S1047-8477(18)30029-7. doi:, 10.1016/j.jsb.2018.02.002. PMID:29428557[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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