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| | ==S177A Kluyveromyces lactis Allophanate Hydrolase== | | ==S177A Kluyveromyces lactis Allophanate Hydrolase== |
| - | <StructureSection load='4ist' size='340' side='right' caption='[[4ist]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4ist' size='340' side='right'caption='[[4ist]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ist]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IST FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ist]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IST FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></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]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4iss|4iss]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0E08119g, KLLA0_E08119g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28985 Candida sphaerica])</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=4ist FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ist OCA], [https://pdbe.org/4ist PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ist RCSB], [https://www.ebi.ac.uk/pdbsum/4ist PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ist ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allophanate_hydrolase Allophanate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.54 3.5.1.54] </span></td></tr>
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| - | <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=4ist FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ist OCA], [http://pdbe.org/4ist PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ist RCSB], [http://www.ebi.ac.uk/pdbsum/4ist PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ist ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q6CP22_KLULA Q6CP22_KLULA] |
| - | Allophanate hydrolase (AH) converts allophanate to ammonium and carbon dioxide. It is conserved in many organisms, and is essential for their utilization of urea as the nitrogen source. It also has important functions in a newly discovered eukaryotic pyrimidine nucleic acid precursor degradation pathway, the yeast-hyphal transition that several pathogens utilize to escape the host defense, and an s-triazine herbicides degradation pathway recently emerged in many soil bacteria. We have determined the crystal structure of the Kluyveromyces lactis AH. Together with structure directed functional studies, we demonstrate that its N and C domains catalyze a two-step reaction, and contribute to maintaining a dimeric form of the enzyme, required for their optimal activities. Our studies also brought molecular insights into their catalytic mechanism. Interestingly, we found that the C domain probably catalyzes a novel form of decarboxylation reaction, which might expand the knowledge of this common reaction in biological systems.
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| - | Structure and Function of Allophanate Hydrolase.,Fan C, Li Z, Yin H, Xiang S J Biol Chem. 2013 Jun 10. PMID:23754281<ref>PMID:23754281</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4ist" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Allophanate hydrolase]] | + | [[Category: Kluyveromyces lactis]] |
| - | [[Category: Candida sphaerica]] | + | [[Category: Large Structures]] |
| - | [[Category: Fan, C]] | + | [[Category: Fan C]] |
| - | [[Category: Xiang, S]] | + | [[Category: Xiang S]] |
| - | [[Category: Allophanate binding]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Mixed alpha and beta structure]]
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