4C9Z

Crystal structure of Siah1 at 1.95 A resolution

Summary for 4C9Z

• Entry DOI: 10.2210/pdb4c9z/pdb
• Descriptor: E3 UBIQUITIN-PROTEIN LIGASE SIAH1, ZINC ION, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: ligase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: Q8IUQ4
• Total number of polymer chains: 2
• Total formula weight: 45054.37

Authors

Rimsa, V.,Eadsforth, T.C.,Hunter, W.N. (deposition date: 2013-10-04, release date: 2013-10-16, Last modification date: 2023-12-20)

Primary citation

Rimsa, V.,Eadsforth, T.C.,Hunter, W.N.
Two High-Resolution Structures of the Human E3 Ubiquitin Ligase Siah1.
Acta Crystallogr.,Sect.F, 96:1339-, 2013

PubMed Abstract: Siah1 is an E3 ubiquitin ligase that contributes to proteasome-mediated degradation of multiple targets in key cellular processes and which shows promise as a therapeutic target in oncology. Structures of a truncated Siah1 bound to peptide-based inhibitors have been reported. Here, new crystallization conditions have allowed the determination of a construct encompassing dual zinc-finger subdomains and substrate-binding domains at significantly higher resolution. Although the crystals appear isomorphous, two structures present distinct states in which the spatial orientation of one zinc-finger subdomain differs with respect to the rest of the dimeric protein. Such a difference, which is indicative of conformational freedom, infers potential biological relevance related to recognition of binding partners. The crystallization conditions and improved models of Siah1 may aid future studies investigating Siah1-ligand complexes.

PubMed: 24316825
DOI: 10.1107/S1744309113031448

Experimental method

X-RAY DIFFRACTION (1.95 Å)