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Structural basis of nonribosomal peptide macrocyclization in fungi

Structural basis of nonribosomal peptide macrocyclization in fungi

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5110376

Structural basis of nonribosomal peptide macrocyclization in fungi

About this item

Full title

Structural basis of nonribosomal peptide macrocyclization in fungi

Publisher

New York: Nature Publishing Group US

Journal title

Nature chemical biology, 2016-12, Vol.12 (12), p.1001-1003

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Unlike their bacterial counterparts, fungal nonribosomal peptide synthetases utilize a terminal condensation-like (C
T
) domain to form macrocycles, details of which are illuminated by structures of a C
T
domain and neighboring thiolation domain.
Nonribosomal peptide synthetases (NRPSs) in fungi biosynthesize important pharmaceutical...

Alternative Titles

Full title

Structural basis of nonribosomal peptide macrocyclization in fungi

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5110376

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5110376

Other Identifiers

ISSN

1552-4450

E-ISSN

1552-4469

DOI

10.1038/nchembio.2202

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