View source for 3rp6


==Crystal Structure of Klebsiella pneumoniae HpxO complexed with FAD==
<StructureSection load='3rp6' size='340' side='right'caption='[[3rp6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rp6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae_MGH_78578 Klebsiella pneumoniae subsp. pneumoniae MGH 78578]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RP6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rp6 OCA], [https://pdbe.org/3rp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rp6 RCSB], [https://www.ebi.ac.uk/pdbsum/3rp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rp6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HPXO_KLEP7 HPXO_KLEP7] Catalyzes the hydroxylation of uric acid to 5-hydroxyisourate.<ref>PMID:19260710</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
HpxO is a flavin-dependent urate oxidase that catalyzes the hydroxylation of uric acid to 5-hydroxyisourate and functions in a novel pathway for purine catabolism found in Klebsiella pneumoniae. We have determined the structures of HpxO with and without uric acid at 2.0 A and 2.2 A, respectively. We have also determined the structure of the R204Q mutant at 2.0 A resolution in the absence of uric acid. The mutant structure is very similar to wild type HpxO except for the conformation of Arg103, which interacts with FAD in the mutant but not in the wild type structure. Interestingly, the R204Q mutation results in the uncoupling of NADH oxidation from uric acid hydroxylation. This suggests that Arg204 facilitates the deprotonation of uric acid activating it for the oxygen transfer. Based on these data, a mechanism for this reaction is proposed consisting of a nucleophilic attack of the urate anion on the flavin hydroperoxide resulting in the formation of 5-hydroxyisourate.

Structural and Mechanistic Studies of HpxO, a Novel FAD-dependent Urate Oxidase from Klebsiella pneumoniae.,Hicks KA, O'Leary SE, Begley TP, Ealick SE Biochemistry. 2012 Dec 21. PMID:23259842<ref>PMID:23259842</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3rp6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae subsp. pneumoniae MGH 78578]]
[[Category: Large Structures]]
[[Category: Begley TP]]
[[Category: Ealick SE]]
[[Category: Hicks KA]]
[[Category: O'Leary SE]]