Unknown

Dataset Information

0

Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL.

ABSTRACT: Lanthipeptides belong to the family of ribosomally synthesized and post-translationally modified peptides (RiPPs) and are subdivided into different classes based on their processing enzymes. The three-domain class IV lanthipeptide synthetases (LanL enzymes) consist of N-terminal lyase, central kinase, and C-terminal cyclase domains. While the catalytic residues of the kinase domains (mediating ATP-dependent Ser/Thr phosphorylations) and the lyase domains (carrying out subsequent phosphoserine/phosphothreonine (pSer/pThr) eliminations to yield dehydroalanine/dehydrobutyrine (Dha/Dhb) residues) have been characterized previously, such studies are missing for LanL cyclase domains. To close this gap of knowledge, this study reports on the identification and validation of the catalytic residues in the cyclase domain of the class IV lanthipeptide synthetase SgbL, which facilitate the nucleophilic attacks by Cys thiols on Dha/Dhb residues for the formation of β-thioether crosslinks.

SUBMITTER: Hegemann JD 

PROVIDER: S-EPMC9292228 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL.

Hegemann Julian D JD   Süssmuth Roderich D RD  

Chembiochem : a European journal of chemical biology 20210912 22

Lanthipeptides belong to the family of ribosomally synthesized and post-translationally modified peptides (RiPPs) and are subdivided into different classes based on their processing enzymes. The three-domain class IV lanthipeptide synthetases (LanL enzymes) consist of N-terminal lyase, central kinase, and C-terminal cyclase domains. While the catalytic residues of the kinase domains (mediating ATP-dependent Ser/Thr phosphorylations) and the lyase domains (carrying out subsequent phosphoserine/ph  ...[more]

Similar Datasets

Unknown One-pot synthesis of class II lanthipeptide bovicin HJ50 via an engineered lanthipeptide synthetase.
| S-EPMC5141572 | biostudies-literature
Unknown Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.
| S-EPMC7305956 | biostudies-literature
Unknown Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.
| S-EPMC10604976 | biostudies-literature
Unknown Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity.
| S-EPMC3212528 | biostudies-literature
Unknown Mechanistic Studies of the Kinase Domains of Class IV Lanthipeptide Synthetases.
| S-EPMC6642009 | biostudies-literature
Unknown Investigation of Substrate Recognition and Biosynthesis in Class IV Lanthipeptide Systems.
| S-EPMC5932250 | biostudies-literature
Unknown Class V Lanthipeptide Cyclase Directs the Biosynthesis of a Stapled Peptide Natural Product.
| S-EPMC9621591 | biostudies-literature
Unknown Discovery and Characterization of a Class IV Lanthipeptide with a Nonoverlapping Ring Pattern.
| S-EPMC7814421 | biostudies-literature
Unknown Crystallization of the class IV adenylyl cyclase from Yersinia pestis.
| S-EPMC2197185 | biostudies-literature
Unknown Identification and characterization of important residues in the catalytic mechanism of CMP-Neu5Ac synthetase from Neisseria meningitidis.
| S-EPMC2901514 | biostudies-literature