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Article

Domain alternation and active site remodeling are conserved structural features of ubiquitin E1.

The Journal of biological chemistry - 21 Jul 2017

Lv Zongyang, Yuan Lingmin, Atkison James H, Aldana-Masangkay Grace, Chen Yuan, Olsen Shaun K

Abstract excerpt

E1 enzymes for ubiquitin (Ub) and Ub-like modifiers (Ubls) harbor two catalytic activities that are required for Ub/Ubl activation: adenylation and thioester bond formation. Structural studies of the E1 for the Ubl small ubiquitin-like modifier (SUMO) revealed a single active site that is transformed by a conformational switch that toggles its competency for catalysis of these two distinct chemical reactions....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 28572513
DOI: 10.1074/jbc.M117.787622
PMCID: PMC5519361

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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