6jls: Difference between revisions
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==Crystal Structure of FMN-dependent Cysteine Decarboxylases TvaF from Thioviridamide Biosynthesis== | |||
<StructureSection load='6jls' size='340' side='right'caption='[[6jls]], [[Resolution|resolution]] 2.24Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_olivoviridis Streptomyces olivoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JLS 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]] 2.24Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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=6jls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jls OCA], [https://pdbe.org/6jls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jls RCSB], [https://www.ebi.ac.uk/pdbsum/6jls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jls ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/T2HUM4_9ACTN T2HUM4_9ACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The biosynthesis of thioviridamide-like compounds has not been elucidated. Herein, we report that TvaF from the thioviridamide biosynthetic gene cluster is an FMN-dependent cysteine decarboxylase that transforms the C-terminal cysteine of precursor peptides into a thioenol motif and exhibits high substrate flexibility. We resolved the crystal structure of TvaF bound with FMN at 2.24 A resolution. Key residues for FMN binding and catalytic activity of TvaF have been identified and evaluated by mutagenesis studies. | |||
Characterization of the FMN-Dependent Cysteine Decarboxylase from Thioviridamide Biosynthesis.,Lu J, Li J, Wu Y, Fang X, Zhu J, Wang H Org Lett. 2019 Jun 3. doi: 10.1021/acs.orglett.9b01531. PMID:31184189<ref>PMID:31184189</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6jls" style="background-color:#fffaf0;"></div> | ||
[[Category: Li | == References == | ||
[[Category: Lu | <references/> | ||
[[Category: Wang | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces olivoviridis]] | |||
[[Category: Li J]] | |||
[[Category: Lu J]] | |||
[[Category: Wang H]] | |||
[[Category: Zhu J]] | |||