Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin

Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin

The enzyme LspA from the human pathogen Staphylococcus aureus (MRSA) contributes to the integrity and function of the bacterial cell envelope. Here, authors provide crystal structures of LspA in complex with two natural antibiotics, which have profoundly different structures but inhibit LspA in an i...

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Main Authors: Samir Olatunji, Xiaoxiao Yu, Jonathan Bailey, Chia-Ying Huang, Marta Zapotoczna, Katherine Bowen, Maja Remškar, Rolf Müller, Eoin M. Scanlan, Joan A. Geoghegan, Vincent Olieric, Martin Caffrey
Format: Article
Language:English
Published: Nature Publishing Group 2020-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-13724-y
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spelling doaj-01038f4ee14b4c098398c5a5008589332021-05-11T09:07:53ZengNature Publishing GroupNature Communications2041-17232020-01-0111111110.1038/s41467-019-13724-yStructures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescinSamir Olatunji0Xiaoxiao Yu1Jonathan Bailey2Chia-Ying Huang3Marta Zapotoczna4Katherine Bowen5Maja Remškar6Rolf Müller7Eoin M. Scanlan8Joan A. Geoghegan9Vincent Olieric10Martin Caffrey11Membrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinMembrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinMembrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinSwiss Light Source, Paul Scherrer InstituteMoyne Institute of Preventive Medicine, Department of Microbiology, School of Genetics and Microbiology, Trinity College DublinSchool of Chemistry, Trinity College DublinDepartment Microbial Natural Products, Helmholtz-Institute for Pharmaceutical Research Saarland, Helmholtz Centre for Infection Research and Department of Pharmacy, Saarland University Campus E8 1Department Microbial Natural Products, Helmholtz-Institute for Pharmaceutical Research Saarland, Helmholtz Centre for Infection Research and Department of Pharmacy, Saarland University Campus E8 1School of Chemistry, Trinity College DublinMoyne Institute of Preventive Medicine, Department of Microbiology, School of Genetics and Microbiology, Trinity College DublinSwiss Light Source, Paul Scherrer InstituteMembrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinThe enzyme LspA from the human pathogen Staphylococcus aureus (MRSA) contributes to the integrity and function of the bacterial cell envelope. Here, authors provide crystal structures of LspA in complex with two natural antibiotics, which have profoundly different structures but inhibit LspA in an identical way.https://doi.org/10.1038/s41467-019-13724-y
collection DOAJ
language English
format Article
sources DOAJ
author Samir Olatunji
Xiaoxiao Yu
Jonathan Bailey
Chia-Ying Huang
Marta Zapotoczna
Katherine Bowen
Maja Remškar
Rolf Müller
Eoin M. Scanlan
Joan A. Geoghegan
Vincent Olieric
Martin Caffrey
spellingShingle Samir Olatunji
Xiaoxiao Yu
Jonathan Bailey
Chia-Ying Huang
Marta Zapotoczna
Katherine Bowen
Maja Remškar
Rolf Müller
Eoin M. Scanlan
Joan A. Geoghegan
Vincent Olieric
Martin Caffrey
Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
Nature Communications
author_facet Samir Olatunji
Xiaoxiao Yu
Jonathan Bailey
Chia-Ying Huang
Marta Zapotoczna
Katherine Bowen
Maja Remškar
Rolf Müller
Eoin M. Scanlan
Joan A. Geoghegan
Vincent Olieric
Martin Caffrey
author_sort Samir Olatunji
title Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
title_short Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
title_full Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
title_fullStr Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
title_full_unstemmed Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
title_sort structures of lipoprotein signal peptidase ii from staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-01-01
description The enzyme LspA from the human pathogen Staphylococcus aureus (MRSA) contributes to the integrity and function of the bacterial cell envelope. Here, authors provide crystal structures of LspA in complex with two natural antibiotics, which have profoundly different structures but inhibit LspA in an identical way.
url https://doi.org/10.1038/s41467-019-13724-y
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