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Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism

Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_30d4da2d31ea4565ae031fba06ccc808

Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism

About this item

Full title

Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2023-08, Vol.14 (1), p.4752-4752, Article 4752

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

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 Cα center of the MslA<...

Alternative Titles

Full title

Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_30d4da2d31ea4565ae031fba06ccc808

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_30d4da2d31ea4565ae031fba06ccc808

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-40232-x

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