|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6jdd' size='340' side='right'caption='[[6jdd]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6jdd' size='340' side='right'caption='[[6jdd]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jdd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chainia_sp. Chainia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JDD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JDD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jdd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JDD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cypD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1931 Chainia sp.])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cypemycin_cysteine_dehydrogenase_(decarboxylating) Cypemycin cysteine dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.36 1.3.99.36] </span></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=6jdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jdd OCA], [https://pdbe.org/6jdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jdd RCSB], [https://www.ebi.ac.uk/pdbsum/6jdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jdd 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=6jdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jdd OCA], [http://pdbe.org/6jdd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jdd RCSB], [http://www.ebi.ac.uk/pdbsum/6jdd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jdd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CYPD_STRSQ CYPD_STRSQ] |
| - | S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) is a unique motif found in several classes of ribosomally synthesized and post-translationally modified peptides (RiPPs). Biosynthesis of AviCys requires flavin-dependent Cys decarboxylases, which are highly divergent among different RiPP classes. In this study, we solved the crystal structure of the cypemycin decarboxylase CypD. We show that CypD is structurally highly similar to lanthipeptide decarboxylases (LanDs) despite the absence of sequence similarities between them. We further show that Cys decarboxylases from four RiPP classes have evolved independently and form two major clusters. These results reveal the convergent evolution of AviCys biosynthesis and suggest that all the flavin-dependent Cys decarboxylases likely have a similar Rossmann fold despite their sequence divergences. This article is protected by copyright. All rights reserved.
| + | |
| - | | + | |
| - | Convergent evolution of the Cys decarboxylases involved in aminovinyl-cysteine (AviCys) biosynthesis.,Mo T, Yuan H, Wang F, Ma S, Wang J, Li T, Liu G, Yu S, Tan X, Ding W, Zhang Q FEBS Lett. 2019 Feb 16. doi: 10.1002/1873-3468.13341. PMID:30771247<ref>PMID:30771247</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6jdd" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chainia sp]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Yuan, H]] | + | [[Category: Streptomyces sp]] |
| - | [[Category: Zhang, Q]] | + | [[Category: Yuan H]] |
| - | [[Category: Biosynthetic protein]] | + | [[Category: Zhang Q]] |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Linaridin]]
| + | |
| - | [[Category: Ripp]]
| + | |
