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==A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and Arg== | ==A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and Arg== | ||
<StructureSection load='4b68' size='340' side='right' caption='[[4b68]], [[Resolution|resolution]] 2.29Å' scene=''> | <StructureSection load='4b68' size='340' side='right' caption='[[4b68]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b68]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4b68]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B68 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b63|4b63]], [[4b64|4b64]], [[4b65|4b65]], [[4b66|4b66]], [[4b67|4b67]], [[4b69|4b69]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b63|4b63]], [[4b64|4b64]], [[4b65|4b65]], [[4b66|4b66]], [[4b67|4b67]], [[4b69|4b69]]</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=4b68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b68 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b68 RCSB], [http://www.ebi.ac.uk/pdbsum/4b68 PDBsum]</span></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=4b68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b68 OCA], [http://pdbe.org/4b68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b68 RCSB], [http://www.ebi.ac.uk/pdbsum/4b68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b68 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 15: | Line 16: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4b68" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aspfm]] | ||
[[Category: Fedkenheuer, M]] | [[Category: Fedkenheuer, M]] | ||
[[Category: Franceschini, S]] | [[Category: Franceschini, S]] | ||
Revision as of 16:34, 11 August 2016
A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and ArgA. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and Arg
Structural highlights
Publication Abstract from PubMedSidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N(5)-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The crystal structures of SidA in complex with ornithine and lysine reveal the geometry of the interactions among flavin, NADP(+), and the substrate amine group that underlie the hydroxylation reaction. The structural elucidation of the enzyme in complex with arginine provides insight into the role of electrostatics and hydrogen bonding in the mechanism of oxygen activation in this family of enzymes. Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases.,Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A Biochemistry. 2012 Sep 11;51(36):7043-5. Epub 2012 Aug 30. PMID:22928747[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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