3an1: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (10 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of rat D428A mutant, urate bound form== | |||
<StructureSection load='3an1' size='340' side='right'caption='[[3an1]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3an1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AN1 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]] 1.73Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=URC:URIC+ACID'>URC</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=3an1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3an1 OCA], [https://pdbe.org/3an1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3an1 RCSB], [https://www.ebi.ac.uk/pdbsum/3an1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3an1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/XDH_RAT XDH_RAT] Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.<ref>PMID:17301076</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Two contradictory models have been proposed for the binding mode of the substrate xanthine to and its activation mechanism by xanthine oxidoreductase. In an effort to distinguish between the two models, we determined the crystal structures of the urate complexes of the demolybdo-form of the D428A mutant of rat xanthine oxidoreductase at 1.7 A and of the reduced bovine milk enzyme at 2.1 A, the latter representing a reaction intermediate. The results clearly indicate the catalytically relevant binding mode of the substrate xanthine. | |||
Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate.,Okamoto K, Kawaguchi Y, Eger BT, Pai EF, Nishino T J Am Chem Soc. 2010 Nov 15. PMID:21077683<ref>PMID:21077683</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3an1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Xanthine dehydrogenase 3D structures|Xanthine dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Eger BT]] | |||
[[Category: Kawaguchi Y]] | |||
[[Category: Nishino T]] | |||
[[Category: Okamoto K]] | |||
[[Category: Pai EF]] | |||
Latest revision as of 17:30, 1 November 2023
Crystal structure of rat D428A mutant, urate bound formCrystal structure of rat D428A mutant, urate bound form
Structural highlights
FunctionXDH_RAT Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.[1] Publication Abstract from PubMedTwo contradictory models have been proposed for the binding mode of the substrate xanthine to and its activation mechanism by xanthine oxidoreductase. In an effort to distinguish between the two models, we determined the crystal structures of the urate complexes of the demolybdo-form of the D428A mutant of rat xanthine oxidoreductase at 1.7 A and of the reduced bovine milk enzyme at 2.1 A, the latter representing a reaction intermediate. The results clearly indicate the catalytically relevant binding mode of the substrate xanthine. Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate.,Okamoto K, Kawaguchi Y, Eger BT, Pai EF, Nishino T J Am Chem Soc. 2010 Nov 15. PMID:21077683[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||