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| | <StructureSection load='7cyx' size='340' side='right'caption='[[7cyx]], [[Resolution|resolution]] 2.41Å' scene=''> | | <StructureSection load='7cyx' size='340' side='right'caption='[[7cyx]], [[Resolution|resolution]] 2.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7cyx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CYX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7CYX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7cyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CYX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.41Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC_0747 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7cyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cyx OCA], [http://pdbe.org/7cyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7cyx RCSB], [http://www.ebi.ac.uk/pdbsum/7cyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7cyx 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=7cyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cyx OCA], [https://pdbe.org/7cyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cyx RCSB], [https://www.ebi.ac.uk/pdbsum/7cyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cyx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q81HQ7_BACCR Q81HQ7_BACCR] |
| | <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: Baccr]] | + | [[Category: Bacillus cereus ATCC 14579]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim K-J]] |
| - | [[Category: Seok, J]] | + | [[Category: Seok J]] |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Oxidase]]
| + | |
| Structural highlights
Function
Q81HQ7_BACCR
Publication Abstract from PubMed
Glycine oxidase (GO) is an enzyme that catalyzes the oxidation of the primary and secondary amines of various chemicals, including glycine, and the enzyme has been applied in a variety of fields, such as biosensor and genetically modified glyphosate resistance plants. Here, we report that the gene product of BC0747 from Bacillus cereus (BcGO) shows oxidase activity for glycine and small d-amino acids, such as d-proline and d-alanine. We also determined the crystal structure of BcGO complexed with the FAD cofactor at a 2.36 A resolution and revealed how the cofactor binds to the deep pocket of the enzyme. We performed the molecular docking calculation of the glycine substrate to the BcGO structure and identified how the carboxyl- and amine-groups of the d-amino acid are stabilized at the substrate binding site. Structural analysis of BcGO also provided information on the structural basis for the stereospecificity of the enzyme to d-amino acids. In addition, we placed the glyphosate molecule, a plant herbicide, at the substrate binding site, and explained how the mutation of Gly51 to arginine enhances enzyme activity.
Structural basis for stereospecificity to d-amino acid of glycine oxidase from Bacillus cereus ATCC 14579.,Seok J, Kim YJ, Kim IK, Kim KJ Biochem Biophys Res Commun. 2020 Sep 26. pii: S0006-291X(20)31846-5. doi:, 10.1016/j.bbrc.2020.09.093. PMID:32993959[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seok J, Kim YJ, Kim IK, Kim KJ. Structural basis for stereospecificity to d-amino acid of glycine oxidase from Bacillus cereus ATCC 14579. Biochem Biophys Res Commun. 2020 Sep 26. pii: S0006-291X(20)31846-5. doi:, 10.1016/j.bbrc.2020.09.093. PMID:32993959 doi:http://dx.doi.org/10.1016/j.bbrc.2020.09.093
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