8uo7

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'''Unreleased structure'''
 
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The entry 8uo7 is ON HOLD until Paper Publication
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==Bovine trypsin in complex with deacetylated wild type microviridin J==
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<StructureSection load='8uo7' size='340' side='right'caption='[[8uo7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8uo7" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Microcystis aeruginosa MRC]]
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[[Category: Bruner SD]]
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[[Category: Chen W]]

Current revision

Bovine trypsin in complex with deacetylated wild type microviridin J

PDB ID 8uo7

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