4P22

Crystal Structure of N-terminal Fragments of E1

Summary for 4P22

• Entry DOI: 10.2210/pdb4p22/pdb
• Descriptor: Ubiquitin-like modifier-activating enzyme 1 (2 entities in total)
• Functional Keywords: e1, ubiquitin, ligase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 96915.84

Authors

Xie, S.-T. (deposition date: 2014-02-28, release date: 2015-02-25, Last modification date: 2023-12-27)

Primary citation

Xie, S.T.
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1).
Biosci.Biotechnol.Biochem., 78:1542-1549, 2014

PubMed Abstract: Ubiquitin-activating enzyme (E1) is a key regulator in protein ubiquitination, which lies on the upstream of the ubiquitin-related pathways and determines the activation of the downstream enzyme cascade. Thus far, no structural information about the human ubiquitin-activating enzyme has been reported. We expressed and purified the N-terminal domains of human E1 and determined their crystal structures, which contain inactive adenylation domain (IAD) and the first catalytic cysteine half-domain (FCCH). This study presents the crystal structure of human E1 fragment for the first time. The main structure of both IAD and FCCH superimposed well with their corresponding domains in yeast Uba1, but their relative positions vary significantly. This work provides new structural insights in understanding the mechanisms of ubiquitin activation in humans.

PubMed: 25209502
DOI: 10.1080/09168451.2014.923301

Experimental method

X-RAY DIFFRACTION (2.75 Å)