View source for 5vws


==Ligand free structure of Cytochrome P450 TbtJ1==
<StructureSection load='5vws' size='340' side='right'caption='[[5vws]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vws]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobispora_bispora_DSM_43833 Thermobispora bispora DSM 43833]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VWS 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]] 2.411&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=5vws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vws OCA], [https://pdbe.org/5vws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vws RCSB], [https://www.ebi.ac.uk/pdbsum/5vws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vws ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D6Y4Z8_THEBD D6Y4Z8_THEBD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thiopeptides are a growing class of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. Many biosynthetic enzymes for RiPPs, especially thiopeptides, are promiscuous and can accept a wide range of peptide substrates with different amino acid sequences; thus, these enzymes have been used as tools to generate new natural product derivatives. Here, we explore an alternative route to molecular complexity by engineering thiopeptide tailoring enzymes to do new or non-native chemistry. We explore cytochrome P450 enzymes as biocatalysts for cyclopropanation of dehydroalanines, chemical motifs found widely in thiopeptides and other RiPP-based natural products. We find that P450TbtJ1 and P450TbtJ2 selectively cyclopropanate dehydroalanines in a number of complex thiopeptide-based substrates and convert them into 1-amino-2-cyclopropane carboxylic acids (ACCAs), which are important pharmacophores. This chemistry takes advantage of the innate affinity of these biosynthetic enzymes for their substrates and enables incorporation of new pharmacophores into thiopeptide architectures. This work also presents a strategy for diversification of natural products through rationally repurposing biosynthetic enzymes as non-natural biocatalysts.

P450-Mediated Non-natural Cyclopropanation of Dehydroalanine-Containing Thiopeptides.,Gober JG, Ghodge SV, Bogart JW, Wever WJ, Watkins RR, Brustad EM, Bowers AA ACS Chem Biol. 2017 Jul 21;12(7):1726-1731. doi: 10.1021/acschembio.7b00358. Epub, 2017 Jun 1. PMID:28535034<ref>PMID:28535034</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vws" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermobispora bispora DSM 43833]]
[[Category: Bowers AA]]
[[Category: Brustad EM]]
[[Category: Ghodge SV]]
[[Category: Gober JG]]