Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51466PINIT domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51466
The Siz/PIAS RING family of SUMO E3 ligases structure reveals a modular architecture that includes an N-terminal PINIT domain, a central SP-RING domain (see <PDOC51044>), and a unique C-terminal domain (SP-CTD). The N-terminal PINIT domain is formed by two antiparallel β sheets; one includes β1, β2, β4, and β9, and the other includes β3, β5, and β8 (see <PDB:3I2D; A>). The β sheets are connected by protruding loops (L1, L2, and L3) that join strands β2-3, β4-5, and β8-9 at one end of the molecule, while β3-4 and β5-8 are connected by α helix α1 and a loop, respectively, on the opposite surface [1].
Most E3 ligases achieve substrate specificity by recruiting the E2~Ub/Ubl thioester and substrate into a complex to promote conjugation. The PINIT domain serves as a scaffold to coordinate PCNA to promote SUMO conjugation to both consensus and nonconsensus lysine side chains [1].
The profile we developed covers the entire PINIT domain.
Last update:October 2009 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Yunus A.A. Lima C.D. |
| Title | Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. | |
| Source | Mol. Cell 35:669-682(2009). | |
| PubMed ID | 19748360 | |
| DOI | 10.1016/j.molcel.2009.07.013 |
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