3gsy
From Proteopedia
(Difference between revisions)
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==Structure of berberine bridge enzyme in complex with dehydroscoulerine== | ==Structure of berberine bridge enzyme in complex with dehydroscoulerine== | ||
- | <StructureSection load='3gsy' size='340' side='right' caption='[[3gsy]], [[Resolution|resolution]] 1.63Å' scene=''> | + | <StructureSection load='3gsy' size='340' side='right'caption='[[3gsy]], [[Resolution|resolution]] 1.63Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3gsy]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3gsy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/California_poppy California poppy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GSY FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DEH:2,9-DIHYDROXY-3,10-DIMETHOXY-5,6-DIHYDROISOQUINO[3,2-A]ISOQUINOLINIUM'>DEH</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DEH:2,9-DIHYDROXY-3,10-DIMETHOXY-5,6-DIHYDROISOQUINO[3,2-A]ISOQUINOLINIUM'>DEH</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d2d|3d2d]], [[3d2h|3d2h]], [[3d2j|3d2j]], [[3fw9|3fw9]], [[3fw7|3fw7]], [[3fw8|3fw8]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3d2d|3d2d]], [[3d2h|3d2h]], [[3d2j|3d2j]], [[3fw9|3fw9]], [[3fw7|3fw7]], [[3fw8|3fw8]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBE1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBE1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 California poppy])</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gsy OCA], [https://pdbe.org/3gsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gsy RCSB], [https://www.ebi.ac.uk/pdbsum/3gsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gsy ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA]] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 3gsy" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3gsy" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Reticuline oxidase|Reticuline oxidase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: California poppy]] | [[Category: California poppy]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Reticuline oxidase]] | [[Category: Reticuline oxidase]] | ||
[[Category: Gruber, K]] | [[Category: Gruber, K]] |
Revision as of 07:53, 16 March 2022
Structure of berberine bridge enzyme in complex with dehydroscoulerine
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Categories: California poppy | Large Structures | Reticuline oxidase | Gruber, K | Macheroux, P | Winkler, A | Alkaloid metabolism | Bicovalent flavinylation | Complex with dehydroscoulerine | Cytoplasmic vesicle | Fad | Flavoprotein | Glycoprotein | N-glycosylation | Oxidoreductase | P-cresol methyl hydroxylase superfamily