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Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification...

Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_nrf_kci_oai_kci_go_kr_ARTI_816655

Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules

About this item

Full title

Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules

Publisher

Seoul: The Microbiological Society of Korea

Journal title

The Journal of Microbiology, 2015, 53(10), , pp.711-717

Language

English

Formats

Publication information

Publisher

Seoul: The Microbiological Society of Korea

More information

Scope and Contents

Contents

Lon proteases degrade defective or denature proteins as well as some folded proteins for the control of cellular protein quality. There are two types of Lon proteases, LonA and LonB. Each consists of two functional components: a protease component and an ATPase associated with various cellular activities (AAA+ module). Here, we report the 2.03 —res...

Alternative Titles

Full title

Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_nrf_kci_oai_kci_go_kr_ARTI_816655

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_nrf_kci_oai_kci_go_kr_ARTI_816655

Other Identifiers

ISSN

1225-8873

E-ISSN

1976-3794

DOI

10.1007/s12275-015-5417-5

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