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| | <StructureSection load='6oh9' size='340' side='right'caption='[[6oh9]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6oh9' size='340' side='right'caption='[[6oh9]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6oh9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OH9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6oh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OH9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GUD1, YDL238C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanine_deaminase Guanine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.3 3.5.4.3] </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=6oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oh9 OCA], [https://pdbe.org/6oh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oh9 RCSB], [https://www.ebi.ac.uk/pdbsum/6oh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oh9 ProSAT]</span></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=6oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oh9 OCA], [http://pdbe.org/6oh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/6oh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oh9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GUAD_YEAST GUAD_YEAST]] Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.<ref>PMID:15565584</ref> | + | [https://www.uniprot.org/uniprot/GUAD_YEAST GUAD_YEAST] Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.<ref>PMID:15565584</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6oh9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6oh9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Deaminase 3D structures|Deaminase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| - | [[Category: Guanine deaminase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: French, J B]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Shek, R S]] | + | [[Category: French JB]] |
| - | [[Category: Amidohydrolase guanine deaminase purine metabolism]] | + | [[Category: Shek RS]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
GUAD_YEAST Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.[1]
Publication Abstract from PubMed
Guanine deaminase is a metabolic enzyme, found in all forms of life, which catalyzes the conversion of guanine to xanthine. Despite the availability of several crystal structures, the molecular determinants of substrate orientation and mechanism remain to be elucidated for the amidohydrolase family of guanine deaminase enzymes. Here, we report the crystal structures of Escherichia coli and Saccharomyces cerevisiae guanine deaminase enzymes (EcGuaD and Gud1, respectively), both members of the amidohydrolase superfamily. EcGuaD and Gud1 retain the overall TIM barrel tertiary structure conserved among amidohydrolase enzymes. Both proteins also possess a single zinc cation with trigonal bipyrimidal coordination geometry within their active sites. We also determined a liganded structure of Gud1 bound to the product, xanthine. Analysis of this structure, along with kinetic data of native and site-directed mutants of EcGuaD, identifies several key residues that are responsible for substrate recognition and catalysis. In addition, after a small library of compounds had been screened, two guanine derivatives, 8-azaguanine and 1-methylguanine, were identified as EcGuaD substrates. Interestingly, both EcGuaD and Gud1 also exhibit secondary ammeline deaminase activity. Overall, this work details key structural features of substrate recognition and catalysis of the amidohydrolase family of guanine deaminase enzymes in support of our long-term goal to engineer these enzymes with altered activity and substrate specificity.
Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily.,Shek R, Hilaire T, Sim J, French JB Biochemistry. 2019 Jul 19. doi: 10.1021/acs.biochem.9b00341. PMID:31283204[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Saint-Marc C, Daignan-Fornier B. GUD1 (YDL238c) encodes Saccharomyces cerevisiae guanine deaminase, an enzyme expressed during post-diauxic growth. Yeast. 2004 Dec;21(16):1359-63. doi: 10.1002/yea.1186. PMID:15565584 doi:http://dx.doi.org/10.1002/yea.1186
- ↑ Shek R, Hilaire T, Sim J, French JB. Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily. Biochemistry. 2019 Jul 19. doi: 10.1021/acs.biochem.9b00341. PMID:31283204 doi:http://dx.doi.org/10.1021/acs.biochem.9b00341
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