8uo7: Difference between revisions
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==Bovine trypsin in complex with deacetylated wild type microviridin J== | |||
<StructureSection load='8uo7' size='340' side='right'caption='[[8uo7]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8uo7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Microcystis_aeruginosa_MRC Microcystis aeruginosa MRC]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UO7 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8uo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8uo7 OCA], [https://pdbe.org/8uo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8uo7 RCSB], [https://www.ebi.ac.uk/pdbsum/8uo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8uo7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Engineering biosynthetic pathways to ribosomally synthesized and post-translationally modified peptides (RiPPs) offers several advantages for both in vivo and in vitro applications. Here we probe the ability of peptide cyclases to generate trimacrocycle microviridin analogs with non-native cross-links. The results demonstrate that diverse chemistries are tolerated by macrocyclases in the ATP-grasp family and allow for the construction of unique cyclic peptide architectures that retain protease inhibition activity. In addition, cocomplex structures of analogs bound to a model protease were determined, illustrating how changes in functional groups maintain peptide conformation and target binding. | |||
Alternative Linkage Chemistries in the Chemoenzymatic Synthesis of Microviridin-Based Cyclic Peptides.,Patel KP, Chen WT, Delbecq L, Bruner SD Org Lett. 2024 Feb 16;26(6):1138-1142. doi: 10.1021/acs.orglett.3c04045. Epub , 2024 Feb 2. PMID:38306609<ref>PMID:38306609</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8uo7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Microcystis aeruginosa MRC]] | |||
[[Category: Bruner SD]] | |||
[[Category: Chen W]] | |||
Latest revision as of 14:57, 6 November 2024
Bovine trypsin in complex with deacetylated wild type microviridin J
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