8gqa: Difference between revisions

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</table>

== Function ==

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

[https://www.uniprot.org/uniprot/3CP2_STRSQ 3CP2_STRSQ] Inhibits chicken myosin light chain kinase with an IC(50) of 8 M. Does not inhibit bovine cAMP-dependent protein kinase or rat protein kinase C. Antibacterial activity against the Gram-positive bacteria B.subtilis, E.faecium and S.aureus. No antibacterial activity against the Gram-negative bacteria E.coli, K.pneumoniae, P.aeruginosa, P.vulgaris, S.sonnei and S.typhosa. No antifungal activity against C.albicans.<ref>PMID:8689231</ref>

== 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 9: / Line 9: @@
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/A0A4V2TW40_9ACTN A0A4V2TW40_9ACTN]
+[https://www.uniprot.org/uniprot/3CP2_STRSQ 3CP2_STRSQ] Inhibits chicken myosin light chain kinase with an IC(50) of 8 M. Does not inhibit bovine cAMP-dependent protein kinase or rat protein kinase C. Antibacterial activity against the Gram-positive bacteria B.subtilis, E.faecium and S.aureus. No antibacterial activity against the Gram-negative bacteria E.coli, K.pneumoniae, P.aeruginosa, P.vulgaris, S.sonnei and S.typhosa. No antifungal activity against C.albicans.<ref>PMID:8689231</ref>
+<div style="background-color:#fffaf0;">
+== 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 8gqa" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>