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Article

Role of a non-canonical surface of Rad6 in ubiquitin conjugating activity.

Nucleic acids research - 15 Oct 2015

Kumar Pankaj, Magala Pearl, Geiger-Schuller Kathryn R, Majumdar Ananya, Tolman Joel R, Wolberger Cynthia

Abstract excerpt

Rad6 is a yeast E2 ubiquitin conjugating enzyme that monoubiquitinates histone H2B in conjunction with the E3, Bre1, but can non-specifically modify histones on its own. We determined the crystal structure of a Rad6∼Ub thioester mimic, which revealed a network of interactions in the crystal in which the ubiquitin in one conjugate contacts Rad6 in another. The region of Rad6 contacted is located on the distal face...

Topics

Histones
Humans
Models, Molecular
Mutation
Saccharomyces cerevisiae Proteins
Ubiquitin
Ubiquitin-Conjugating Enzymes
Ubiquitination

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 26286193
DOI: 10.1093/nar/gkv845
PMCID: PMC4605308

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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