5ez7

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==Crystal structure of the FAD dependent oxidoreductase PA4991 from Pseudomonas aeruginosa==
==Crystal structure of the FAD dependent oxidoreductase PA4991 from Pseudomonas aeruginosa==
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<StructureSection load='5ez7' size='340' side='right' caption='[[5ez7]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5ez7' size='340' side='right'caption='[[5ez7]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ez7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EZ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EZ7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ez7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EZ7 FirstGlance]. <br>
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</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=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<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=5ez7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ez7 OCA], [http://pdbe.org/5ez7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ez7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ez7 PDBsum]</span></td></tr>
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<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=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ez7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ez7 OCA], [https://pdbe.org/5ez7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ez7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ez7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ez7 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Y4991_PSEAE Y4991_PSEAE] Probably functions as a FAD-dependent oxidoreductase, whose physiological substrate is unknown. Does not display amino-acid oxidase or glycerol-3-phosphate dehydrogenase activities (PubMed:26841760). Is essential for growth of P.aeruginosa in the sputum of cystic fibrosis patients (PubMed:25775563).<ref>PMID:25775563</ref> <ref>PMID:26841760</ref>
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The locus PA4991 in Pseudomonas aeruginosa encodes an open reading frame that has been identified as essential for the virulence and/or survival of this pathogenic organism in the infected host. Here, it is shown that this gene encodes a monomeric FAD-binding protein of molecular mass 42.2 kDa. The structure of PA4991 was determined by a combination of molecular replacement using a search model generated with Rosetta and phase improvement by a low-occupancy heavy-metal derivative. PA4991 belongs to the GR2 family of FAD-dependent oxidoreductases, comprising an FAD-binding domain typical of the glutathione reductase family and a second domain dominated by an eight-stranded mixed beta-sheet. Most of the protein-FAD interactions are via the FAD-binding domain, but the isoalloxazine ring is located at the domain interface and interacts with residues from both domains. A comparison with the structurally related glycine oxidase and glycerol-3-phosphate dehydrogenase shows that in spite of very low amino-acid sequence identity (&lt;18%) several active-site residues involved in substrate binding in these enzymes are conserved in PA4991. However, enzymatic assays show that PA4991 does not display amino-acid oxidase or glycerol-3-phosphate dehydrogenase activities, suggesting that it requires different substrates for activity.
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Crystal structure of the flavoenzyme PA4991 from Pseudomonas aeruginosa.,Jacewicz A, Schnell R, Lindqvist Y, Schneider G Acta Crystallogr F Struct Biol Commun. 2016 Feb 1;72(Pt 2):105-11. doi:, 10.1107/S2053230X15024437. Epub 2016 Jan 22. PMID:26841760<ref>PMID:26841760</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ez7" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Jacewicz, A]]
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[[Category: Large Structures]]
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[[Category: Lindqvist, Y]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Schneider, G]]
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[[Category: Jacewicz A]]
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[[Category: Schnell, R]]
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[[Category: Lindqvist Y]]
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[[Category: Flavine]]
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[[Category: Schneider G]]
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[[Category: Flavoenzyme]]
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[[Category: Schnell R]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal structure of the FAD dependent oxidoreductase PA4991 from Pseudomonas aeruginosa

PDB ID 5ez7

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