Structural insights into early events in the conjugation of ubiquitin and ubiquitin-like proteins

Arthur L Haas

doi:10.1016/j.molcel.2007.07.003

Structural insights into early events in the conjugation of ubiquitin and ubiquitin-like proteins

Mol Cell. 2007 Jul 20;27(2):174-175. doi: 10.1016/j.molcel.2007.07.003.

Author

Arthur L Haas¹

Affiliation

¹ Department of Biochemistry and Molecular Biology, Louisiana State University School of Medicine, 1901 Perdido Street, New Orleans, LA 70112, USA. Electronic address: ahaas@lsuhsc.edu.

PMID: 17643365
DOI: 10.1016/j.molcel.2007.07.003

Abstract

NMR studies of the SUMO-activating enzyme in complex with Ubc9 (Wang et al., 2007, this issue of Molecular Cell) complement a recent crystal structure of Ubc12 bound to the NEDD8-activating enzyme ternary complex (Huang et al., 2007), elucidating details of the first steps in the conjugation of ubiquitin and ubiquitin-like proteins.

Publication types

Comment
Review

MeSH terms

Humans
Molecular Structure
Multiprotein Complexes
Nuclear Magnetic Resonance, Biomolecular
Ubiquitin / chemistry*
Ubiquitin / metabolism*
Ubiquitins / chemistry*
Ubiquitins / metabolism*

Substances

Multiprotein Complexes
Ubiquitin
Ubiquitins