6jls: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6jls is ~~ON HOLD until Paper~~ Publication

==Crystal Structure of FMN-dependent Cysteine Decarboxylases TvaF from Thioviridamide Biosynthesis==

== Structural highlights ==

<table><tr><td colspan='2'>[[6jls]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JLS FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jls OCA], [http://pdbe.org/6jls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jls RCSB], [http://www.ebi.ac.uk/pdbsum/6jls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jls ProSAT]</span></td></tr>

</table>

== 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.

~~Authors: Li, J~~., Lu, J., ~~Wang~~, H., Zhu, J.

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>

~~Description: Crystal Structure~~ of ~~FMN~~-~~dependent Cysteine Decarboxylases TvaF from Thioviridamide Biosynthesis~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

~~[[Category: Zhu, J~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Li, J]]

[[Category: Lu, J]]

[[Category: Wang, H]]

[[Category: Zhu, J]]

[[Category: Biosynthetic protein]]

[[Category: Fmn-dependent]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6jls is ON HOLD  until Paper Publication
+==Crystal Structure of FMN-dependent Cysteine Decarboxylases TvaF from Thioviridamide Biosynthesis==
+<StructureSection load='6jls' size='340' side='right'caption='[[6jls]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6jls]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JLS FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jls OCA], [http://pdbe.org/6jls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jls RCSB], [http://www.ebi.ac.uk/pdbsum/6jls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jls ProSAT]</span></td></tr>
+</table>
+<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.
-Authors: Li, J., Lu, J., Wang, H., Zhu, J.
+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>
-Description: Crystal Structure of FMN-dependent Cysteine Decarboxylases TvaF from Thioviridamide Biosynthesis
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Zhu, J]]
+<div class="pdbe-citations 6jls" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Li, J]]
 [[Category: Lu, J]]
 [[Category: Wang, H]]
+[[Category: Zhu, J]]
+[[Category: Biosynthetic protein]]
+[[Category: Fmn-dependent]]