Structure and tRNA Specificity of MibB, a Lantibiotic Dehydratase from Actinobacteria Involved in NAI-107 Biosynthesis-Reference-Cited by-同舟云学术

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Structure and tRNA Specificity of MibB, a Lantibiotic Dehydratase from Actinobacteria Involved in NAI-107 Biosynthesis

Published:2016-03 Issue:3 Volume:23 Page:370-380
ISSN:2451-9456
Container-title:Cell Chemical Biology
language:en
Short-container-title:Cell Chemical Biology

Author:

Ortega Manuel A.,Hao Yue,Walker Mark C.,Donadio Stefano,Sosio Margherita,Nair Satish K.,van der Donk Wilfred A.

Funder

National Institutes of Health

European Commission

NIGMS-NIH Chemistry-Biology Interface

Ford Foundation

Department of Biochemistry

Publisher

Elsevier BV

Subject

Clinical Biochemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,Biochemistry

Reference48 articles.

1. Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature;Arnison;Nat. Prod. Rep.,2013

2. A prevalent peptide-binding domain guides ribosomal natural product biosynthesis;Burkhart;Nat. Chem. Biol.,2015

3. Determining the structure and mode of action of microbisporicin, a potent lantibiotic active against multiresistant pathogens;Castiglione;Chem. Biol.,2008

4. Lacticin 481 synthetase phosphorylates its substrate during lantibiotic production;Chatterjee;J. Am. Chem. Soc.,2005

5. Biosynthesis and mode of action of lantibiotics;Chatterjee;Chem. Rev.,2005

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