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TldD/TldE peptidases and N-deacetylases: A structurally unique yet ubiquitous protein family in the microbial metabolism
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SYSNO ASEP 0562368 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title TldD/TldE peptidases and N-deacetylases: A structurally unique yet ubiquitous protein family in the microbial metabolism Author(s) Vobruba, Šimon (MBU-M)
Kadlčík, Stanislav (MBU-M) RID, ORCID
Janata, Jiří (MBU-M) RID, ORCID
Kameník, Zdeněk (MBU-M) RID, ORCIDArticle number 127186 Source Title Microbiological Research. - : Elsevier - ISSN 0944-5013
Roč. 265, Dec (2022)Number of pages 9 s. Language eng - English Country DE - Germany Keywords Deacetylases ; Lincosamides ; Microbial specialized metabolism ; Peptidases ; Protein structure ; Ribosomally synthesized post-translationally modified peptides ; TldD/TldE Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects GJ20-09811Y GA ČR - Czech Science Foundation (CSF) LX22NPO5103 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000863959500006 EID SCOPUS 85138452106 DOI 10.1016/j.micres.2022.127186 Annotation Here we provide a review on TldD/TldE family proteins, summarizing current knowledge and outlining further research perspectives. Despite being widely distributed in bacteria and archaea, TldD/TldE proteins have been escaping attention for a long time until several recent reports pointed to their unique features. Specifically, TldD/TldE generally act as peptidases, though some of them turned out to be N-deacetylases. Biological function of TldD/TldE has been extensively described in bacterial specialized metabolism, in which they participate in the biosynthesis of lincosamide antibiotics (as N-deacetylases), and in the biosynthesis of ribosomally synthesized and post-translationally modified bioactive peptides (as peptidases). These enzymes possess special position in the relevant biosynthesis since they convert non-bioactive intermediates into bioactive metabolites. Further, based on a recent study of Escherichia coli TldD/TldE, these heterodimeric metallopeptidases possess a new protein fold exhibiting several structural features with no precedent in the Protein Data Bank. The most interesting ones are structural elements forming metal-containing active site on the inner surface of the catalytically active subunit TldD, in which substrates bind through β sheet interactions in the sequence-independent manner. It results in relaxed substrate specificity of TldD/TldE, which is counterbalanced by enclosing the active centre within the hollow core of the heterodimer and only appropriate substrates can entry through a narrow channel. Based on the published data, we hypothesize a yet unrecognized central metabolic function of TldD/TldE in the degradation of (partially) unfolded proteins, i.e., in protein quality control. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2023 Electronic address https://www.sciencedirect.com/science/article/pii/S0944501322002269?via%3Dihub
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