View source for 4b67


==A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and ornithine==
<StructureSection load='4b67' size='340' side='right' caption='[[4b67]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4b67]] 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=4B67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B67 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</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]], [[4b68|4b68]], [[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=4b67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b67 OCA], [http://pdbe.org/4b67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b67 RCSB], [http://www.ebi.ac.uk/pdbsum/4b67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b67 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SidA 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<ref>PMID:22928747</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4b67" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspfm]]
[[Category: Fedkenheuer, M]]
[[Category: Franceschini, S]]
[[Category: Mattevi, A]]
[[Category: Robinson, H H]]
[[Category: Sobrado, P]]
[[Category: Vogelaar, N J]]
[[Category: Oxidoreductase]]
[[Category: Siderophore]]