1r4m
From Proteopedia
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APPBP1-UBA3-NEDD8, an E1-ubiquitin-like protein complex
Overview
E1 enzymes initiate ubiquitin-like protein (ubl) transfer cascades by, catalyzing adenylation of the ubl's C terminus. An E1's selectivity for, its cognate ubl is essential because the E1 subsequently coordinates the, ubl with its correct downstream pathway. We report here the structure of, the 120 kDa quaternary complex between human APPBP1-UBA3, a heterodimeric, E1, its ubl NEDD8, and ATP. The E1 selectively recruits NEDD8 through a, bipartite interface, involving a domain common to all ubl activating, enzymes including bacterial ancestors, and also eukaryotic E1-specific, sequences. By modeling ubiquitin into the NEDD8 binding site and, performing mutational analysis, we identify a single conserved arginine in, APPBP1-UBA3 that acts as a selectivity gate, preventing misactivation of, ubiquitin by NEDD8's E1. NEDD8 residues that interact with E1 correspond, to residues in ubiquitin important for binding the proteasome and other, ubiquitin-interacting proteins, suggesting that the conjugation and, recognition machineries have coevolved for each specific ubl.
About this Structure
1R4M is a Protein complex structure of sequences from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1., Walden H, Podgorski MS, Huang DT, Miller DW, Howard RJ, Minor DL Jr, Holton JM, Schulman BA, Mol Cell. 2003 Dec;12(6):1427-37. PMID:14690597
Page seeded by OCA on Mon Nov 12 19:00:06 2007
