2dyt
From Proteopedia
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The crystal structure of Saccharomyces cerevisiae Atg3
Overview
Atg3 is an E2-like enzyme that catalyzes the conjugation of Atg8 and, phosphatidylethanolamine (PE). The Atg8-PE conjugate is essential for, autophagy, which is the bulk degradation process of cytoplasmic components, by the vacuolar/lysosomal system. We report here the crystal structure of, Saccharomyces cerevisiae Atg3 at 2.5-A resolution. Atg3 has an, alpha/beta-fold, and its core region is topologically similar to canonical, E2 enzymes. Atg3 has two regions inserted in the core region, one of which, consists of approximately 80 residues and has a random coil structure in, solution and another with a long alpha-helical structure that protrudes, from the core region as far as 30 A. In vivo and in vitro analyses, suggested that the former region is responsible for binding Atg7, an, E1-like enzyme, and that the latter is responsible for binding Atg8. A, sulfate ion was bound near the catalytic cysteine of Atg3, suggesting a, possible binding site for the phosphate moiety of PE. The structure of, Atg3 provides a molecular basis for understanding the unique lipidation, reaction that Atg3 carries out.
About this Structure
2DYT is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation., Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F, J Biol Chem. 2007 Mar 16;282(11):8036-43. Epub 2007 Jan 16. PMID:17227760
Page seeded by OCA on Wed Nov 21 09:52:10 2007
