Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility.

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Title: Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility.
Authors: Reimer JM; Department of Biochemistry and Center de Recherche en Biologie Structurale, McGill University, Montréal, QC H3G 0B1, Canada., Eivaskhani M; Department of Biochemistry and Center de Recherche en Biologie Structurale, McGill University, Montréal, QC H3G 0B1, Canada., Harb I; Department of Biochemistry and Center de Recherche en Biologie Structurale, McGill University, Montréal, QC H3G 0B1, Canada., Guarné A; Department of Biochemistry and Center de Recherche en Biologie Structurale, McGill University, Montréal, QC H3G 0B1, Canada., Weigt M; Sorbonne Université, CNRS, Institut de Biologie Paris-Seine, Laboratory of Computational and Quantitative Biology, F-75005 Paris, France., Schmeing TM; Department of Biochemistry and Center de Recherche en Biologie Structurale, McGill University, Montréal, QC H3G 0B1, Canada. martin.schmeing@mcgill.ca.
Source: Science (New York, N.Y.) [Science] 2019 Nov 08; Vol. 366 (6466).
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 0404511 Publication Model: Print Cited Medium: Internet ISSN: 1095-9203 (Electronic) Linking ISSN: 00368075 NLM ISO Abbreviation: Science Subsets: MEDLINE
Database: MEDLINE Ultimate
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Description
ISSN:1095-9203
DOI:10.1126/science.aaw4388