5d9e

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d9e OCA], [http://pdbe.org/5d9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d9e RCSB], [http://www.ebi.ac.uk/pdbsum/5d9e PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d9e OCA], [http://pdbe.org/5d9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d9e RCSB], [http://www.ebi.ac.uk/pdbsum/5d9e PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5d9e" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 10:20, 26 February 2016

Crystal Structure of the Proline-rich Lasso Peptide Caulosegnin II

5d9e, resolution 0.86Å

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