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Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited

Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1777534069

Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited

About this item

Full title

Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited

Publisher

United States: Public Library of Science

Journal title

PloS one, 2016-03, Vol.11 (3), p.e0152075-e0152075

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

The biosynthetic pathway of peptidoglycan, an essential component of bacterial cell wall, is a well-recognized target for antibiotic development. Peptidoglycan precursors are synthesized in the bacterial cytosol by various enzymes including the ATP-hydrolyzing Mur ligases, which catalyze the stepwise addition of amino acids to a UDP-MurNAc precurso...

Alternative Titles

Full title

Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1777534069

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1777534069

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0152075

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