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Crystal Structure and Catalytic Mechanism of the LPS 3-O-Deacylase PagL from Pseudomonas aeruginosa

Crystal Structure and Catalytic Mechanism of the LPS 3-O-Deacylase PagL from Pseudomonas aeruginosa

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1564273

Crystal Structure and Catalytic Mechanism of the LPS 3-O-Deacylase PagL from Pseudomonas aeruginosa

About this item

Full title

Crystal Structure and Catalytic Mechanism of the LPS 3-O-Deacylase PagL from Pseudomonas aeruginosa

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2006-05, Vol.103 (18), p.7071-7076

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Pathogenic Gram-negative bacteria can modify the lipid A portion of their lipopolysaccharide in response to environmental stimuli. 3-O-deacylation of lipid A by the outer membrane enzyme PagL modulates signaling through Toll-like receptor 4, leading to a reduced host immune response. We found that PagL is widely disseminated among Gram-negative bac...

Alternative Titles

Full title

Crystal Structure and Catalytic Mechanism of the LPS 3-O-Deacylase PagL from Pseudomonas aeruginosa

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1564273

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1564273

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0509392103

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