3H1D
Structure of the HUWE1 HECT Domain
Summary for 3H1D
| Entry DOI | 10.2210/pdb3h1d/pdb |
| Related | 1c4z 1nd7 1zvd 2oni 3g1n |
| Descriptor | E3 ubiquitin-protein ligase HUWE1, SULFATE ION (3 entities in total) |
| Functional Keywords | e3ligase, ubiquitin, hect, lobe, alternative splicing, chromosomal rearrangement, cytoplasm, differentiation, disease mutation, dna-binding, ligase, mental retardation, nucleus, phosphoprotein, ubl conjugation pathway |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q7Z6Z7 |
| Total number of polymer chains | 1 |
| Total formula weight | 47808.86 |
| Authors | Partridge, J.R.,Schwartz, T.U. (deposition date: 2009-04-11, release date: 2009-12-08, Last modification date: 2023-09-06) |
| Primary citation | Pandya, R.K.,Partridge, J.R.,Love, K.R.,Schwartz, T.U.,Ploegh, H.L. A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. J.Biol.Chem., 285:5664-5673, 2010 Cited by PubMed Abstract: E3 ubiquitin ligases catalyze the final step of ubiquitin conjugation and regulate numerous cellular processes. The HECT class of E3 ubiquitin (Ub) ligases directly transfers Ub from bound E2 enzyme to a myriad of substrates. The catalytic domain of HECT Ub ligases has a bilobal architecture that separates the E2 binding region and catalytic site. An important question regarding HECT domain function is the control of ligase activity and specificity. Here we present a functional analysis of the HECT domain of the E3 ligase HUWE1 based on crystal structures and show that a single N-terminal helix significantly stabilizes the HECT domain. We observe that this element modulates HECT domain activity, as measured by self-ubiquitination induced in the absence of this helix, as distinct from its effects on Ub conjugation of substrate Mcl-1. Such subtle changes to the protein may be at the heart of the vast spectrum of substrate specificities displayed by HECT domain E3 ligases. PubMed: 20007713DOI: 10.1074/jbc.M109.051805 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.892 Å) |
Structure validation
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