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3qva
From Proteopedia
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| - | [[ | + | ==Structure of Klebsiella pneumoniae 5-hydroxyisourate hydrolase== |
| + | <StructureSection load='3qva' size='340' side='right' caption='[[3qva]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3qva]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae Klebsiella pneumoniae subsp. pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QVA FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HpxT, KPN78578_16360, KPN_01666 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=72407 Klebsiella pneumoniae subsp. pneumoniae])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qva OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qva RCSB], [http://www.ebi.ac.uk/pdbsum/3qva PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The stereospecific oxidative degradation of uric acid to (S)-allantoin has recently been demonstrated to proceed via two unstable intermediates and requires three separate enzymatic reactions. The second step of this reaction, the conversion of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline, is catalyzed by HIU hydrolase (HIUH). The high-resolution crystal structure of HIUH from the opportunistic pathogen Klebsiella pneumoniae (KpHIUH) has been determined. KpHIUH is a homotetrameric protein that, based on sequence and structural similarity, belongs to the transthyretin-related protein family. In addition, the steady-state kinetic parameters for this enzyme and four active-site mutants have been measured. These data provide valuable insight into the functional roles of the active-site residues. Based upon the structural and kinetic data, a mechanism is proposed for the KpHIUH-catalyzed reaction. | ||
| - | + | Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae.,French JB, Ealick SE Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):671-7. Epub 2011, Jul 12. PMID:21795808<ref>PMID:21795808</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Klebsiella pneumoniae subsp. pneumoniae]] | [[Category: Klebsiella pneumoniae subsp. pneumoniae]] | ||
[[Category: Ealick, S E.]] | [[Category: Ealick, S E.]] | ||
Revision as of 04:39, 5 June 2014
Structure of Klebsiella pneumoniae 5-hydroxyisourate hydrolase
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