3rp8

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Current revision (09:44, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3rp8' size='340' side='right'caption='[[3rp8]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='3rp8' size='340' side='right'caption='[[3rp8]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rp8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klep7 Klep7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RP8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rp8]] 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=3RP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RP8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 1.968&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rp6|3rp6]], [[3rp7|3rp7]]</div></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KPN78578_16330, KPN_01663 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272620 KLEP7])</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=3rp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rp8 OCA], [https://pdbe.org/3rp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rp8 RCSB], [https://www.ebi.ac.uk/pdbsum/3rp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rp8 ProSAT]</span></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=3rp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rp8 OCA], [https://pdbe.org/3rp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rp8 RCSB], [https://www.ebi.ac.uk/pdbsum/3rp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rp8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HPXO_KLEP7 HPXO_KLEP7]] Catalyzes the hydroxylation of uric acid to 5-hydroxyisourate.<ref>PMID:19260710</ref>
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[https://www.uniprot.org/uniprot/HPXO_KLEP7 HPXO_KLEP7] Catalyzes the hydroxylation of uric acid to 5-hydroxyisourate.<ref>PMID:19260710</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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 3rp8" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Klep7]]
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[[Category: Klebsiella pneumoniae subsp. pneumoniae MGH 78578]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Begley, T P]]
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[[Category: Begley TP]]
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[[Category: Ealick, S E]]
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[[Category: Ealick SE]]
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[[Category: Hicks, K A]]
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[[Category: Hicks KA]]
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[[Category: Leary, S E.O]]
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[[Category: O'Leary SE]]
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[[Category: Fad-binding protein]]
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[[Category: Monooxygenase]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of Klebsiella pneumoniae R204Q HpxO complexed with FAD

PDB ID 3rp8

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Proteopedia Page Contributors and Editors (what is this?)

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