View source for 6t70


==Structure of the Bottromycin epimerase BotH in complex with Bottromycin A2 derivative==
<StructureSection load='6t70' size='340' side='right'caption='[[6t70]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6t70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._BC16019 Streptomyces sp. BC16019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T70 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]] 1.58&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MQZ:Bottromycin+A2+derivative'>MQZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6t70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t70 OCA], [https://pdbe.org/6t70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t70 RCSB], [https://www.ebi.ac.uk/pdbsum/6t70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t70 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K4MHV9_9ACTN K4MHV9_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
D-amino acids endow peptides with diverse, desirable properties, but the post-translational and site-specific epimerization of L-amino acids into their D-counterparts is rare and chemically challenging. Bottromycins are ribosomally synthesized and post-translationally modified peptides that have overcome this challenge and feature a D-aspartate (D-Asp), which was proposed to arise spontaneously during biosynthesis. We have identified the highly unusual alpha/beta-hydrolase (ABH) fold enzyme BotH as a peptide epimerase responsible for the post-translational epimerization of L-Asp to D-Asp during bottromycin biosynthesis. The biochemical characterization of BotH combined with the structures of BotH and the BotH-substrate complex allowed us to propose a mechanism for this reaction. Bioinformatic analyses of BotH homologs show that similar ABH enzymes are found in diverse biosynthetic gene clusters. This places BotH as the founding member of a group of atypical ABH enzymes that may be able to epimerize non-Asp stereocenters across different families of secondary metabolites.

The bottromycin epimerase BotH defines a group of atypical alpha/beta-hydrolase-fold enzymes.,Sikandar A, Franz L, Adam S, Santos-Aberturas J, Horbal L, Luzhetskyy A, Truman AW, Kalinina OV, Koehnke J Nat Chem Biol. 2020 Sep;16(9):1013-1018. doi: 10.1038/s41589-020-0569-y. Epub, 2020 Jun 29. PMID:32601484<ref>PMID:32601484</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6t70" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. BC16019]]
[[Category: Koehnke J]]
[[Category: Sikandar A]]