5lv9
From Proteopedia
(Difference between revisions)
m (Protected "5lv9" [edit=sysop:move=sysop]) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of thermophilic tryptophan halogenase (Th-Hal) enzyme from Streptomycin violaceusniger.== | |
| + | <StructureSection load='5lv9' size='340' side='right'caption='[[5lv9]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lv9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_violaceusniger Streptomyces violaceusniger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LV9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33Å</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=5lv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lv9 OCA], [https://pdbe.org/5lv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lv9 RCSB], [https://www.ebi.ac.uk/pdbsum/5lv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lv9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1L1QK36_STRVO A0A1L1QK36_STRVO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Flavin-dependent halogenase (Fl-Hal) enzymes have been shown to halogenate a range of synthetic as well as natural aromatic compounds. The exquisite regioselectively of Fl-Hal enzymes can provide halogenated building blocks which are inaccessible using standard halogenation chemistries. Consequently, Fl-Hal are potentially useful biocatalysts for the chemoenzymatic synthesis of pharmaceuticals and other valuable products, which are derived from haloaromatic precursors. However, the application of Fl-Hal enzymes, in vitro, has been hampered by their poor catalytic activity and lack of stability. To overcome these issues, we identified a thermophilic tryptophan halogenase (Th-Hal), which has significantly improved catalytic activity and stability, compared with other Fl-Hal characterised to date. When used in combination with a thermostable flavin reductase, Th-Hal can efficiently halogenate a number of aromatic substrates. X-ray crystal structures of Th-Hal, and the reductase partner (Th-Fre), provide insights into the factors that contribute to enzyme stability, which could guide the discovery and engineering of more robust and productive halogenase biocatalysts. | ||
| - | + | Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes.,Menon BR, Latham J, Dunstan MS, Brandenburger E, Klemstein U, Leys D, Karthikeyan C, Greaney MF, Shepherd SA, Micklefield J Org Biomol Chem. 2016 Oct 4;14(39):9354-9361. PMID:27714222<ref>PMID:27714222</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Dunstan | + | <div class="pdbe-citations 5lv9" style="background-color:#fffaf0;"></div> |
| - | [[Category: Menon | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces violaceusniger]] | ||
| + | [[Category: Dunstan MS]] | ||
| + | [[Category: Menon B]] | ||
Current revision
Crystal structure of thermophilic tryptophan halogenase (Th-Hal) enzyme from Streptomycin violaceusniger.
| |||||||||||
