2fzp
From Proteopedia
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'''Crystal structure of the USP8 interaction domain of human NRDP1''' | '''Crystal structure of the USP8 interaction domain of human NRDP1''' | ||
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[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
[[Category: Xue, S.]] | [[Category: Xue, S.]] | ||
| - | [[Category: | + | [[Category: E3 ligase]] |
| - | [[Category: | + | [[Category: Protein ubiquitination]] |
| - | [[Category: | + | [[Category: Sgc]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Structural genomics consortium]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:30:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:30, 4 May 2008
Crystal structure of the USP8 interaction domain of human NRDP1
Overview
Ubiquitin-specific protease 8 (USP8) hydrolyzes mono and polyubiquitylated targets such as epidermal growth factor receptors and is involved in clathrin-mediated internalization. In 1182 residues, USP8 contains multiple domains, including coiled-coil, rhodanese, and catalytic domains. We report the first high-resolution crystal structures of these domains and discuss their implications for USP8 function. The amino-terminal domain is a homodimer with a novel fold. It is composed of two five-helix bundles, where the first helices are swapped, and carboxyl-terminal helices are extended in an antiparallel fashion. The structure of the rhodanese domain, determined in complex with the E3 ligase NRDP1, reveals the canonical rhodanese fold but with a distorted primordial active site. The USP8 recognition domain of NRDP1 has a novel protein fold that interacts with a conserved peptide loop of the rhodanese domain. A consensus sequence of this loop is found in other NRDP1 targets, suggesting a common mode of interaction. The structure of the carboxyl-terminal catalytic domain of USP8 exhibits the conserved tripartite architecture but shows unique traits. Notably, the active site, including the ubiquitin binding pocket, is in a closed conformation, incompatible with substrate binding. The presence of a zinc ribbon subdomain near the ubiquitin binding site further suggests a polyubiquitin-specific binding site and a mechanism for substrate induced conformational changes.
About this Structure
2FZP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)., Avvakumov GV, Walker JR, Xue S, Finerty PJ Jr, Mackenzie F, Newman EM, Dhe-Paganon S, J Biol Chem. 2006 Dec 8;281(49):38061-70. Epub 2006 Oct 11. PMID:17035239 Page seeded by OCA on Sun May 4 04:30:46 2008
Categories: Homo sapiens | Single protein | Arrowsmith, C. | Avvakumov, G V. | Bochkarev, A. | Butler-Cole, C. | Dhe-Paganon, S. | Edwards, A. | Jr., P J.Finerty. | Newman, E M. | SGC, Structural Genomics Consortium. | Sundstrom, M. | Walker, J R. | Weigelt, J. | Xue, S. | E3 ligase | Protein ubiquitination | Sgc | Structural genomic | Structural genomics consortium
