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Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase.

ABSTRACT: The artificial WSTF PHD_EL5 RING finger was designed via "?-helical region substitution", and its structural model for the attachment of activated ubiquitin has been demonstrated. Chemical modifications of Cys residues, the circular dichroism spectra, and substrate-independent ubiquitination assays illustrated that the WSTF PHD_EL5 RING finger has E3 activity, and it is ubiquitinated via Lys14. Homology modeling calculations revealed that the WSTF PHD_EL5 RING finger possesses a classical RING fold for specific E2-E3 binding. The docking poses of the WSTF PHD_EL5 RING finger with the UbcH5b-ubiquitin conjugate provided insight into its functional E2 interaction and development of ubiquitination at the atomic level. The structural model of the artificial WSTF PHD_EL5 RING finger proposed by the present work is useful and may help to extend the strategy of ?-helical region substitution.

SUBMITTER: Miyamoto K

PROVIDER: S-EPMC4192618 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase.

Miyamoto Kazuhide K

Scientific reports 20141010

The artificial WSTF PHD_EL5 RING finger was designed via "α-helical region substitution", and its structural model for the attachment of activated ubiquitin has been demonstrated. Chemical modifications of Cys residues, the circular dichroism spectra, and substrate-independent ubiquitination assays illustrated that the WSTF PHD_EL5 RING finger has E3 activity, and it is ubiquitinated via Lys14. Homology modeling calculations revealed that the WSTF PHD_EL5 RING finger possesses a classical RING f ...[more]

PMID: 25300604

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