7cyx
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7cyx is ON HOLD until Paper Publication Authors: Seok, J., Kim, K.-J. Description: Crystal strcuture of Glycine oxidase from Bacillus cereus ATCC 1...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal strcuture of Glycine oxidase from Bacillus cereus ATCC 14579== | |
| + | <StructureSection load='7cyx' size='340' side='right'caption='[[7cyx]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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'>[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> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q81HQ7_BACCR Q81HQ7_BACCR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:32993959</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7cyx" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus cereus ATCC 14579]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kim K-J]] | ||
| + | [[Category: Seok J]] | ||
Current revision
Crystal strcuture of Glycine oxidase from Bacillus cereus ATCC 14579
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