Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ
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Publisher
New York: Nature Publishing Group US
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Language
English
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New York: Nature Publishing Group US
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Contents
HtrA proteins have chaperone and protease activities, but how they bind and fold their substrates is poorly understood. New cryo-EM analyses of a protease-defective bacterial DegQ mutant in complex with several different substrates provide a structural model of HtrA proteins in their chaperone mode.
The HtrA protein family combines chaperone and...
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Full title
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3272482
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3272482
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ISSN
1545-9993
E-ISSN
1545-9985
DOI
10.1038/nsmb.2210
