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EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure amo...

EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure amo...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_904486233

EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure among helix-turn-helix proteins

About this item

Full title

EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure among helix-turn-helix proteins

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2011-08, Vol.108 (33), p.13450-13455

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

EspR is a transcriptional regulator that activates the ESX-1 secretion system during Mycobacterium tuberculosis infection and is critical for pathogenesis. It is unique among DNA-binding proteins as it is secreted as part of a feedback regulatory loop that serves to mitigate transcriptional activity. Here we report the crystal structure of a functi...

Alternative Titles

Full title

EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure among helix-turn-helix proteins

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_904486233

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_904486233

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1110242108

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