3ruj | pdb_00003ruj

Crystal Structure of N-terminal region of yeast Atg7

spinqualitylabelsall models 3ruj, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ruj is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Autophagy is the degradation of cellular organelles via the lysosomal pathway. The autophagic ubiquitin-like (Ubl) molecule Atg8 is activated by the E1-like enzyme Atg7. As this noncanonical E1 enzyme's domain organization is unique among Ubl-activating E1 enzymes, the structural basis for its interactions with Atg8 and partner E2 enzymes remains obscure. Here we present the structure of the N-terminal domain of Atg7, revealing a unique protein fold and interactions with both autophagic E2 enzymes Atg3 and Atg10. The structure of the C-terminal domain of Atg7 in complex with Atg8 shows the mode of dimerization and mechanism of recognition of Atg8. Notably, the catalytic cysteine residue in Atg7 is positioned close to the C-terminal glycine of Atg8, its target for thioester formation, potentially eliminating the need for large conformational rearrangements characteristic of other E1s. Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8.,Hong SB, Kim BW, Lee KE, Kim SW, Jeon H, Kim J, Song HK Nat Struct Mol Biol. 2011 Nov 6. doi: 10.1038/nsmb.2165. PMID:22056771 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Autophagy-related protein 3D structures

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