1Q5W
Ubiquitin Recognition by Npl4 Zinc-Fingers
Summary for 1Q5W
Entry DOI | 10.2210/pdb1q5w/pdb |
Related | 1NJ3 |
Descriptor | homolog of yeast nuclear protein localization 4, Ubiquitin, ZINC ION (3 entities in total) |
Functional Keywords | ubiquitin, protein-protein complex, zinc-finger, rubredoxin knuckle, nzf domain, protein binding |
Biological source | Rattus norvegicus (Norway rat) More |
Cellular location | Cytoplasm, cytosol: Q9ES54 |
Total number of polymer chains | 2 |
Total formula weight | 12019.10 |
Authors | Alam, S.L.,Sun, J.,Payne, M.,Welch, B.D.,Blake, B.K.,Davis, D.R.,Meyer, H.H.,Emr, S.D.,Sundquist, W.I. (deposition date: 2003-08-11, release date: 2004-03-30, Last modification date: 2024-05-22) |
Primary citation | Alam, S.L.,Sun, J.,Payne, M.,Welch, B.D.,Blake, B.K.,Davis, D.R.,Meyer, H.H.,Emr, S.D.,Sundquist, W.I. Ubiquitin interactions of NZF zinc fingers. Embo J., 23:1411-1421, 2004 Cited by PubMed Abstract: Ubiquitin (Ub) functions in many different biological pathways, where it typically interacts with proteins that contain modular Ub recognition domains. One such recognition domain is the Npl4 zinc finger (NZF), a compact zinc-binding module found in many proteins that function in Ub-dependent processes. We now report the solution structure of the NZF domain from Npl4 in complex with Ub. The structure reveals that three key NZF residues (13TF14/M25) surrounding the zinc coordination site bind the hydrophobic 'Ile44' surface of Ub. Mutations in the 13TF14/M25 motif inhibit Ub binding, and naturally occurring NZF domains that lack the motif do not bind Ub. However, substitution of the 13TF14/M25 motif into the nonbinding NZF domain from RanBP2 creates Ub-binding activity, demonstrating the versatility of the NZF scaffold. Finally, NZF mutations that inhibit Ub binding by the NZF domain of Vps36/ESCRT-II also inhibit sorting of ubiquitylated proteins into the yeast vacuole. Thus, the NZF is a versatile protein recognition domain that is used to bind ubiquitylated proteins during vacuolar protein sorting, and probably many other biological processes. PubMed: 15029239DOI: 10.1038/sj.emboj.7600114 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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