5ig8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of macrocyclase MdnB from Microcystis aeruginosa MRC== | |
| + | <StructureSection load='5ig8' size='340' side='right'caption='[[5ig8]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ig8]] is a 2 chain structure with sequence from [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=5IG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IG8 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]] 2.278Å</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=5ig8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ig8 OCA], [https://pdbe.org/5ig8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ig8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ig8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ig8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B2G3C9_MICAE B2G3C9_MICAE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Macrocyclization is a common feature of natural product biosynthetic pathways including the diverse family of ribosomal peptides. Microviridins are architecturally complex cyanobacterial ribosomal peptides that target proteases with potent reversible inhibition. The product structure is constructed via three macrocyclizations catalyzed sequentially by two members of the ATP-grasp family, a unique strategy for ribosomal peptide macrocyclization. Here we describe in detail the structural basis for the enzyme-catalyzed macrocyclizations in the microviridin J pathway of Microcystis aeruginosa. The macrocyclases MdnC and MdnB interact with a conserved alpha-helix of the precursor peptide using a novel precursor-peptide recognition mechanism. The results provide insight into the unique protein-protein interactions that are key to the chemistry, suggest an origin for the natural combinatorial synthesis of microviridin peptides, and provide a framework for future engineering efforts to generate designed compounds. | ||
| - | + | Structural basis for precursor protein-directed ribosomal peptide macrocyclization.,Li K, Condurso HL, Li G, Ding Y, Bruner SD Nat Chem Biol. 2016 Nov;12(11):973-979. doi: 10.1038/nchembio.2200. Epub 2016 Sep, 26. PMID:27669417<ref>PMID:27669417</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5ig8" style="background-color:#fffaf0;"></div> |
| - | [[Category: Condurso | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Microcystis aeruginosa MRC]] | ||
| + | [[Category: Bruner SD]] | ||
| + | [[Category: Condurso HL]] | ||
| + | [[Category: Li K]] | ||
Current revision
Crystal structure of macrocyclase MdnB from Microcystis aeruginosa MRC
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