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Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferas...

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferas...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5544336

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase

About this item

Full title

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2017-07, Vol.114 (30), p.E6044-E6053

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Gram-negative bacteria express a diverse array of lipoproteins that are essential for various aspects of cell growth and virulence, including nutrient uptake, signal transduction, adhesion, conjugation, sporulation, and outer membrane protein folding. Lipoprotein maturation requires the sequential activity of three enzymes that are embedded in the...

Alternative Titles

Full title

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5544336

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5544336

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1707813114

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