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| | <StructureSection load='5hft' size='340' side='right'caption='[[5hft]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='5hft' size='340' side='right'caption='[[5hft]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hft]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Klep7 Klep7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HFT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hft]] is a 4 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=5HFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HFT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KPN_01768 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272620 KLEP7])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.646Å</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=5hft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hft OCA], [http://pdbe.org/5hft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hft RCSB], [http://www.ebi.ac.uk/pdbsum/5hft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hft 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=5hft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hft OCA], [https://pdbe.org/5hft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hft RCSB], [https://www.ebi.ac.uk/pdbsum/5hft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hft ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HPXW_KLEP7 HPXW_KLEP7] Involved in the uric acid degradation pathway. Catalyzes the conversion of oxamate to oxalate.<ref>PMID:27303801</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Klep7]] | + | [[Category: Klebsiella pneumoniae subsp. pneumoniae MGH 78578]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Ealick SE]] |
| - | [[Category: Hicks, K A]] | + | [[Category: Hicks KA]] |
| - | [[Category: Amidohydrolase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
HPXW_KLEP7 Involved in the uric acid degradation pathway. Catalyzes the conversion of oxamate to oxalate.[1]
Publication Abstract from PubMed
HpxW from the ubiquitous pathogen Klebsiella pneumoniae is involved in a novel uric acid degradation pathway downstream from the formation of oxalurate. Specifically, HpxW is an oxamate amidohydrolase which catalyzes the conversion of oxamate to oxalate and is a member of the Ntn-hydrolase superfamily. HpxW is autoprocessed from an inactive precursor to form a heterodimer, resulting in a 35.5 kDa alpha subunit and a 20 kDa beta subunit. Here, the structure of HpxW is presented and the substrate complex is modeled. In addition, the steady-state kinetics of this enzyme and two active-site variants were characterized. These structural and biochemical studies provide further insight into this class of enzymes and allow a mechanism for catalysis consistent with other members of the Ntn-hydrolase superfamily to be proposed.
Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway.,Hicks KA, Ealick SE Acta Crystallogr D Struct Biol. 2016 Jun 1;72(Pt 6):808-16. doi:, 10.1107/S2059798316007099. Epub 2016 May 25. PMID:27303801[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hicks KA, Ealick SE. Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol. 2016 Jun 1;72(Pt 6):808-16. doi:, 10.1107/S2059798316007099. Epub 2016 May 25. PMID:27303801 doi:http://dx.doi.org/10.1107/S2059798316007099
- ↑ Hicks KA, Ealick SE. Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol. 2016 Jun 1;72(Pt 6):808-16. doi:, 10.1107/S2059798316007099. Epub 2016 May 25. PMID:27303801 doi:http://dx.doi.org/10.1107/S2059798316007099
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