5ez7: Difference between revisions
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==Crystal structure of the FAD dependent oxidoreductase PA4991 from Pseudomonas aeruginosa== | |||
<StructureSection load='5ez7' size='340' side='right' caption='[[5ez7]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
<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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 (<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ez7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Jacewicz, A]] | [[Category: Jacewicz, A]] | ||
[[Category: Lindqvist, Y]] | [[Category: Lindqvist, Y]] | ||
[[Category: Schneider, G]] | [[Category: Schneider, G]] | ||
[[Category: Schnell, R]] | |||
[[Category: Flavine]] | |||
[[Category: Flavoenzyme]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 02:39, 21 February 2016
Crystal structure of the FAD dependent oxidoreductase PA4991 from Pseudomonas aeruginosa
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