6bzz: Difference between revisions
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<StructureSection load='6bzz' size='340' side='right'caption='[[6bzz]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='6bzz' size='340' side='right'caption='[[6bzz]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bzz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BZZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[6bzz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Psef5 Psef5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BZZ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pltM, PFL_2784 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220664 PSEF5])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkylhalidase Alkylhalidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.1 3.8.1.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkylhalidase Alkylhalidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.1 3.8.1.1] </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=6bzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzz OCA], [http://pdbe.org/6bzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bzz RCSB], [http://www.ebi.ac.uk/pdbsum/6bzz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzz 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=6bzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzz OCA], [http://pdbe.org/6bzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bzz RCSB], [http://www.ebi.ac.uk/pdbsum/6bzz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Controlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural products, such as terbutaline, fenoterol, resveratrol, and catechin. Crystal structures of PltM in complex with phloroglucinol and FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of this halogenase. | |||
Unusual substrate and halide versatility of phenolic halogenase PltM.,Mori S, Pang AH, Thamban Chandrika N, Garneau-Tsodikova S, Tsodikov OV Nat Commun. 2019 Mar 19;10(1):1255. doi: 10.1038/s41467-019-09215-9. PMID:30890712<ref>PMID:30890712</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6bzz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Alkylhalidase]] | [[Category: Alkylhalidase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Psef5]] | |||
[[Category: Garneau-Tsodikova, S]] | [[Category: Garneau-Tsodikova, S]] | ||
[[Category: Pang, A H]] | [[Category: Pang, A H]] | ||
Revision as of 11:09, 3 April 2019
Crystal structure of halogenase PltM in complex with partially bound FADCrystal structure of halogenase PltM in complex with partially bound FAD
Structural highlights
Publication Abstract from PubMedControlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural products, such as terbutaline, fenoterol, resveratrol, and catechin. Crystal structures of PltM in complex with phloroglucinol and FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of this halogenase. Unusual substrate and halide versatility of phenolic halogenase PltM.,Mori S, Pang AH, Thamban Chandrika N, Garneau-Tsodikova S, Tsodikov OV Nat Commun. 2019 Mar 19;10(1):1255. doi: 10.1038/s41467-019-09215-9. PMID:30890712[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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