Atg12–Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site
Atg12–Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site
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New York: Nature Publishing Group US
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English
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New York: Nature Publishing Group US
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In the yeast autophagy system, the Atg12–Atg5 conjugate acts as an E3 to promote the E2 activity of Atg3, which conjugates Atg8 to phosphatidylethanolamine. Now structural and biochemical analyses reveal that Atg12–Atg5 induces a rearrangement in the catalytic center of Atg3, which employs a threonine residue in addition to the active cysteine to c...
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Atg12–Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site
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TN_cdi_proquest_miscellaneous_1324385431
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1324385431
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ISSN
1545-9993
E-ISSN
1545-9985
DOI
10.1038/nsmb.2527
