5d9e
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of the Proline-rich Lasso Peptide Caulosegnin II== | |
| + | <StructureSection load='5d9e' size='340' side='right'caption='[[5d9e]], [[Resolution|resolution]] 0.86Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5d9e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_segnis_ATCC_21756 Caulobacter segnis ATCC 21756]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D9E 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]] 0.859Å</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=SME:METHIONINE+SULFOXIDE'>SME</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=5d9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d9e OCA], [https://pdbe.org/5d9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d9e RCSB], [https://www.ebi.ac.uk/pdbsum/5d9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d9e ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D5VKJ8_CAUST D5VKJ8_CAUST] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lasso peptides are fascinating natural products with a unique structural fold that can exhibit tremendous thermal stability. Here, we investigate factors responsible for the thermal stability of caulosegnin II. By employing X-ray crystallography, mutational analysis and molecular dynamics simulations, the ring residue proline 8 was proven to be crucial for thermal stability. | ||
| - | + | The ring residue proline 8 is crucial for the thermal stability of the lasso peptide caulosegnin II.,Hegemann JD, Fage CD, Zhu S, Harms K, Di Leva FS, Novellino E, Marinelli L, Marahiel MA Mol Biosyst. 2016 Feb 11. PMID:26863937<ref>PMID:26863937</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5d9e" style="background-color:#fffaf0;"></div> |
| - | [[Category: Harms | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Marahiel | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Caulobacter segnis ATCC 21756]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fage CD]] | ||
| + | [[Category: Harms K]] | ||
| + | [[Category: Hegemann JD]] | ||
| + | [[Category: Marahiel MA]] | ||
Current revision
Crystal Structure of the Proline-rich Lasso Peptide Caulosegnin II
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