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4iss
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==SeMet-substituted Kluyveromyces lactis Allophanate Hydrolase== | |
| + | <StructureSection load='4iss' size='340' side='right'caption='[[4iss]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4iss]] 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=4ISS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ISS FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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=4iss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iss OCA], [https://pdbe.org/4iss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iss RCSB], [https://www.ebi.ac.uk/pdbsum/4iss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iss ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6CP22_KLULA Q6CP22_KLULA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4iss" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kluyveromyces lactis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fan C]] | ||
| + | [[Category: Xiang S]] | ||
Current revision
SeMet-substituted Kluyveromyces lactis Allophanate Hydrolase
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