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Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_733855449

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

About this item

Full title

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2010-04, Vol.17 (4), p.471-478

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

The bacterial protease ClpP forms an active complex with Clp-ATPases, but can also be directly activated by a recently characterized class of antibiotics (ADEP). Now the crystal structures of
Bacillus subtilis
ClpP bound to ADEPs reveal the conformational changes involved in ClpP's activation.
Clp-family proteins are prototypes for studyin...

Alternative Titles

Full title

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_733855449

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_733855449

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/nsmb.1787

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