8itg: Difference between revisions

Line 8:

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8itg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8itg OCA], [https://pdbe.org/8itg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8itg RCSB], [https://www.ebi.ac.uk/pdbsum/8itg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8itg ProSAT]</span></td></tr>

</table>

== ~~Function~~ ==

~~[https~~://~~www~~.~~uniprot~~.~~org~~/~~uniprot~~/~~A0A4V2TW40_9ACTN A0A4V2TW40_9ACTN]~~

== Publication Abstract from PubMed ==

The lasso peptide MS-271 is a ribosomally synthesized and post-translationally modified peptide (RiPP) consisting of 21 amino acids with D-tryptophan at the C-terminus, and is derived from the precursor peptide MslA. MslH, encoded in the MS-271 biosynthetic gene cluster (msl), catalyzes the epimerization at the Calpha center of the MslA C-terminal Trp21, leading to epi-MslA. The detailed catalytic process, including the catalytic site and cofactors, has remained enigmatic. Herein, based on X-ray crystallographic studies in association with MslA core peptide analogues, we show that MslH is a metallo-dependent peptide epimerase with a calcineurin-like fold. The crystal structure analysis, followed by site-directed mutagenesis, docking simulation, and ICP-MS studies demonstrate that MslH employs acid/base chemistry to facilitate the reversible epimerization of the C-terminal Trp21 of MslA, by utilizing two pairs of His/Asp catalytic residues that are electrostatically tethered to a six-coordination motif with a Ca(II) ion via water molecules.

Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism.,Nakashima Y, Kawakami A, Ogasawara Y, Maeki M, Tokeshi M, Dairi T, Morita H Nat Commun. 2023 Aug 8;14(1):4752. doi: 10.1038/s41467-023-40232-x. PMID:37550286<ref>PMID:37550286</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8itg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8itg OCA], [https://pdbe.org/8itg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8itg RCSB], [https://www.ebi.ac.uk/pdbsum/8itg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8itg ProSAT]</span></td></tr>
 </table>
-== Function ==
+<div style="background-color:#fffaf0;">
-[https://www.uniprot.org/uniprot/A0A4V2TW40_9ACTN A0A4V2TW40_9ACTN]
+== Publication Abstract from PubMed ==
+The lasso peptide MS-271 is a ribosomally synthesized and post-translationally modified peptide (RiPP) consisting of 21 amino acids with D-tryptophan at the C-terminus, and is derived from the precursor peptide MslA. MslH, encoded in the MS-271 biosynthetic gene cluster (msl), catalyzes the epimerization at the Calpha center of the MslA C-terminal Trp21, leading to epi-MslA. The detailed catalytic process, including the catalytic site and cofactors, has remained enigmatic. Herein, based on X-ray crystallographic studies in association with MslA core peptide analogues, we show that MslH is a metallo-dependent peptide epimerase with a calcineurin-like fold. The crystal structure analysis, followed by site-directed mutagenesis, docking simulation, and ICP-MS studies demonstrate that MslH employs acid/base chemistry to facilitate the reversible epimerization of the C-terminal Trp21 of MslA, by utilizing two pairs of His/Asp catalytic residues that are electrostatically tethered to a six-coordination motif with a Ca(II) ion via water molecules.
+Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism.,Nakashima Y, Kawakami A, Ogasawara Y, Maeki M, Tokeshi M, Dairi T, Morita H Nat Commun. 2023 Aug 8;14(1):4752. doi: 10.1038/s41467-023-40232-x. PMID:37550286<ref>PMID:37550286</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 8itg" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>