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Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4.

ABSTRACT: Ubiquitylated proteins are directed into a large number of different cellular pathways through interactions with effector proteins that contain conserved ubiquitin binding motifs. Here, we report the solution structure and ubiquitin binding properties of one such motif, the Npl4 zinc finger or RanBP2/Nup358 zinc finger (NZF) domain. Npl4 NZF forms a compact module composed of four antiparallel beta-strands linked by three ordered loops. A single zinc ion is coordinated by four conserved cysteines from the first and third loops, which form two rubredoxin knuckles. Npl4 NZF binds specifically, but weakly, to free ubiquitin using a conserved 13TF14 dipeptide to interact with the "Ile-44" surface of ubiquitin. Our studies reveal the structure of this versatile class of protein binding domains and provide a means for identifying the subset of NZF domains likely to bind ubiquitin.

SUBMITTER: Wang B

PROVIDER: S-EPMC3366119 | biostudies-literature | 2003 May

REPOSITORIES: biostudies-literature

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Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4.

Wang Bin B Alam Steven L SL Meyer Hemmo H HH Payne Marielle M Stemmler Timothy L TL Davis Darrell R DR Sundquist Wesley I WI

The Journal of biological chemistry 20030318 22

Ubiquitylated proteins are directed into a large number of different cellular pathways through interactions with effector proteins that contain conserved ubiquitin binding motifs. Here, we report the solution structure and ubiquitin binding properties of one such motif, the Npl4 zinc finger or RanBP2/Nup358 zinc finger (NZF) domain. Npl4 NZF forms a compact module composed of four antiparallel beta-strands linked by three ordered loops. A single zinc ion is coordinated by four conserved cysteine ...[more]

PMID: 12644454

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