2KR1
Solution NMR structure of zinc binding N-terminal domain of ubiquitin-protein ligase E3A from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HR3662
Summary for 2KR1
| Entry DOI | 10.2210/pdb2kr1/pdb |
| NMR Information | BMRB: 16620 |
| Descriptor | Ubiquitin protein ligase E3A, ZINC ION (2 entities in total) |
| Functional Keywords | ligase, ubl conjugation pathway, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, structural genomics consortium (sgc) |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 9477.12 |
| Authors | Lemak, A.,Yee, A.,Fares, C.,Semesi, A.,Xiao, R.,Montelione, G.,Dhe-Paganon, S.,Arrowsmith, C.,Northeast Structural Genomics Consortium (NESG),Structural Genomics Consortium (SGC) (deposition date: 2009-11-27, release date: 2009-12-22, Last modification date: 2024-11-06) |
| Primary citation | Lemak, A.,Yee, A.,Bezsonova, I.,Dhe-Paganon, S.,Arrowsmith, C.H. Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A. J.Biomol.Nmr, 51:185-190, 2011 Cited by PubMed Abstract: Ube3A (also referred to as E6AP for E6 Associated Protein) is a E3 ubiquitin-protein ligase implicated in the development of Angelman syndrome by controlling degradation of synaptic protein Arc and oncogenic papilloma virus infection by controlling degradation of p53. This article describe the solution NMR structure of the conserved N-terminal domain of human Ube3A (residues 24-87) that contains two residues (Cys44 and Arg62) found to be mutated in patients with Angelman syndrome. The structure of this domain adopts a novel Zn-binding fold we called AZUL (Amino-terminal Zn-finger of Ube3a Ligase). The AZUL domain has a helix-loop-helix architecture with a Zn ion coordinated by four Cys residues arranged in Cys-X(4)-Cys-X(4)-Cys-X(28)-Cys motif. Three of the Zn-bound residues are located in a 23-residue long and well structured loop that connects two α-helicies. PubMed: 21947926DOI: 10.1007/s10858-011-9552-y PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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