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3d2h
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3d2h.png|left|200px]] | ||
| - | < | + | ==Structure of berberine bridge enzyme from Eschscholzia californica, monoclinic crystal form== |
| - | + | <StructureSection load='3d2h' size='340' side='right'caption='[[3d2h]], [[Resolution|resolution]] 1.65Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3d2h]] 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=3D2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D2H 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>, <scene name='pdbligand=FSH:(2R,3S,4S)-5-[(4R)-6,7-dimethyl-2,3,5-trioxo-1H-spiro[imidazolidine-4,2-quinoxalin]-4(3H)-yl]-2,3,4-trihydroxypentyl-adenosine+diphosphate'>FSH</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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]], [[3d2j|3d2j]]</div></td></tr> |
| - | + | <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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=3d2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2h OCA], [https://pdbe.org/3d2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d2h RCSB], [https://www.ebi.ac.uk/pdbsum/3d2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/3d2h_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3d2h ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Berberine bridge enzyme catalyzes the conversion of (S)-reticuline to (S)-scoulerine by formation of a carbon-carbon bond between the N-methyl group and the phenolic ring. We elucidated the structure of berberine bridge enzyme from Eschscholzia californica and determined the kinetic rates for three active site protein variants. Here we propose a catalytic mechanism combining base-catalyzed proton abstraction with concerted carbon-carbon coupling accompanied by hydride transfer from the N-methyl group to the N5 atom of the FAD cofactor. | ||
| - | + | A concerted mechanism for berberine bridge enzyme.,Winkler A, Lyskowski A, Riedl S, Puhl M, Kutchan TM, Macheroux P, Gruber K Nat Chem Biol. 2008 Dec;4(12):739-41. Epub 2008 Oct 26. PMID:18953357<ref>PMID:18953357</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3d2h" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Reticuline oxidase|Reticuline oxidase]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: California poppy]] |
| - | + | [[Category: Large Structures]] | |
| - | + | ||
| - | == | + | |
| - | + | ||
| - | [[Category: | + | |
[[Category: Reticuline oxidase]] | [[Category: Reticuline oxidase]] | ||
| - | [[Category: | + | [[Category: Gruber, K]] |
| - | [[Category: | + | [[Category: Lyskowski, A]] |
| + | [[Category: Macheroux, P]] | ||
| + | [[Category: Winkler, A]] | ||
[[Category: Alakloid biosynthesis]] | [[Category: Alakloid biosynthesis]] | ||
[[Category: Bi-covalent flavinylation]] | [[Category: Bi-covalent flavinylation]] | ||
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[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: P-cresol methylhydroxylase superfamily]] | [[Category: P-cresol methylhydroxylase superfamily]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 24 20:49:21 2008'' | ||
Current revision
Structure of berberine bridge enzyme from Eschscholzia californica, monoclinic crystal form
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