6f32
From Proteopedia
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<StructureSection load='6f32' size='340' side='right' caption='[[6f32]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='6f32' size='340' side='right' caption='[[6f32]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6f32]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F32 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6f32]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_rochei"_(berger_et_al._1953)_preobrazhenskaya_et_al._in_gauze_et_al._1957 "actinomyces rochei" (berger et al. 1953) preobrazhenskaya et al. in gauze et al. 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F32 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CJ8:(2~{R},3~{R})-2,3-bis(oxidanyl)-~{N},~{N}-dipropyl-butanediamide'>CJ8</scene>, <scene name='pdbligand=CJE:ethyl+(2~{R})-2-methyl-3-oxidanylidene-butanoate'>CJE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CJ8:(2~{R},3~{R})-2,3-bis(oxidanyl)-~{N},~{N}-dipropyl-butanediamide'>CJ8</scene>, <scene name='pdbligand=CJE:ethyl+(2~{R})-2-methyl-3-oxidanylidene-butanoate'>CJE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lkcE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1928 "Actinomyces rochei" (Berger et al. 1953) Preobrazhenskaya et al. in Gauze et al. 1957])</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=6f32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f32 OCA], [http://pdbe.org/6f32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f32 RCSB], [http://www.ebi.ac.uk/pdbsum/6f32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f32 ProSAT]</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=6f32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f32 OCA], [http://pdbe.org/6f32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f32 RCSB], [http://www.ebi.ac.uk/pdbsum/6f32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f32 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acquisition of new catalytic activity is a relatively rare evolutionary event. A striking example appears in the pathway to the antibiotic lankacidin, as a monoamine oxidase (MAO) family member, LkcE, catalyzes both an unusual amide oxidation, and a subsequent intramolecular Mannich reaction to form the polyketide macrocycle. We report evidence here for the molecular basis for this dual activity. The reaction sequence involves several essential active site residues and a conformational change likely comprising an interdomain hinge movement. These features, which have not previously been described in the MAO family, both depend on a unique dimerization mode relative to all structurally characterized members. Taken together, these data add weight to the idea that designing new multifunctional enzymes may require changes in both architecture and catalytic machinery. Encouragingly, however, our data also show LkcE to bind alternative substrates, supporting its potential utility as a general cyclization catalyst in synthetic biology. | ||
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| + | Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis.,Dorival J, Risser F, Jacob C, Collin S, Drager G, Paris C, Chagot B, Kirschning A, Gruez A, Weissman KJ Nat Commun. 2018 Sep 28;9(1):3998. doi: 10.1038/s41467-018-06323-w. PMID:30266997<ref>PMID:30266997</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6f32" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:35, 10 October 2018
Crystal structure of a dual function amine oxidase/cyclase in complex with substrate analogues
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Categories: Chagot, B | Collin, S | Dorival, J | Drager, G | Gruez, A | Jacob, C | Kirschning, A | Paris, C | Risser, F | Weissman, K J | Amine oxydase | Cyclase | Flavoprotein | Post-pks enzyme | Tayloring enzyme
