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| | ==Berberine bridge enzyme G164A variant, a reticuline dehydrogenase== | | ==Berberine bridge enzyme G164A variant, a reticuline dehydrogenase== |
| - | <StructureSection load='4pzf' size='340' side='right' caption='[[4pzf]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4pzf' size='340' side='right'caption='[[4pzf]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pzf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/California_poppy California poppy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pzf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pve|4pve]], [[4pvh|4pvh]], [[4pvj|4pvj]], [[4pvk|4pvk]], [[4pwb|4pwb]], [[4pwc|4pwc]], [[3d2h|3d2h]]</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=4pzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzf OCA], [https://pdbe.org/4pzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzf RCSB], [https://www.ebi.ac.uk/pdbsum/4pzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzf ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 California poppy])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pzf RCSB], [http://www.ebi.ac.uk/pdbsum/4pzf PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4pzf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Reticuline oxidase|Reticuline oxidase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: California poppy]] | + | [[Category: Eschscholzia californica]] |
| - | [[Category: Reticuline oxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Macheroux, P]] | + | [[Category: Macheroux P]] |
| - | [[Category: Steiner, B]] | + | [[Category: Steiner B]] |
| - | [[Category: Wallner, S]] | + | [[Category: Wallner S]] |
| - | [[Category: Zafred, D]] | + | [[Category: Zafred D]] |
| - | [[Category: Berberine bridge-forming enzyme]]
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| - | [[Category: Bi-covalent flavinylation]]
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| - | [[Category: Flavoprotein]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Tetrahydroprotoberberine synthase]]
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| Structural highlights
Function
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.
Publication Abstract from PubMed
The ability of flavoenzymes to reduce dioxygen varies greatly, and is controlled by the protein environment, which may cause either a rapid reaction (oxidases) or a sluggish reaction (dehydrogenases). Previously, a 'gatekeeper' amino acid residue was identified that controls the reactivity to dioxygen in proteins from the vanillyl alcohol oxidase superfamily of flavoenzymes. We have identified an alternative gatekeeper residue that similarly controls dioxygen reactivity in the grass pollen allergen Phl p 4, a member of this superfamily that has glucose dehydrogenase activity and the highest redox potential measured in a flavoenzyme. A substitution at the alternative gatekeeper site (I153V) transformed the enzyme into an efficient oxidase by increasing dioxygen reactivity by a factor of 60 000. An inverse exchange (V169I) in the structurally related berberine bridge enzyme (BBE) decreased its dioxygen reactivity by a factor of 500. Structural and biochemical characterization of these and additional variants showed that our model enzymes possess a cavity that binds an anion and resembles the 'oxyanion hole' in the proximity of the flavin ring. We showed also that steric control of access to this site is the most important parameter affecting dioxygen reactivity in BBE-like enzymes. Analysis of flavin-dependent oxidases from other superfamilies revealed similar structural features, suggesting that dioxygen reactivity may be governed by a common mechanistic principle. DATABASE: Structural data are available in PDB database under the accession numbers 4PVE, 4PVH, 4PVJ, 4PVK, 4PWB, 4PWC and 4PZF .
Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction.,Zafred D, Steiner B, Teufelberger AR, Hromic A, Karplus PA, Schofield CJ, Wallner S, Macheroux P FEBS J. 2015 Jan 24. doi: 10.1111/febs.13212. PMID:25619330[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zafred D, Steiner B, Teufelberger AR, Hromic A, Karplus PA, Schofield CJ, Wallner S, Macheroux P. Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction. FEBS J. 2015 Jan 24. doi: 10.1111/febs.13212. PMID:25619330 doi:http://dx.doi.org/10.1111/febs.13212
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