3PG6

The carboxyl terminal domain of human deltex 3-like

Summary for 3PG6

• Entry DOI: 10.2210/pdb3pg6/pdb
• Descriptor: E3 ubiquitin-protein ligase DTX3L, CITRIC ACID, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: dna-damage, ligase, metal-binding, nucleus, phosphorylation, chromatin regulator, ubl conjugation pathway, zinc-finger, structural genomics consortium, sgc
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q8TDB6
• Total number of polymer chains: 4
• Total formula weight: 72669.95

Authors

Walker, J.R.,Obiero, J.,Kania, J.,Schuler, H.,Bountra, C.,Weigelt, J.,Edwards, A.M.,Arrowsmith, C.H.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (deposition date: 2010-10-30, release date: 2010-12-01, Last modification date: 2024-02-21)

Primary citation

Obiero, J.,Walker, J.R.,Dhe-Paganon, S.
Fold of the conserved DTC domain in Deltex proteins.
Proteins, 80:1495-1499, 2012

PubMed Abstract: Human Deltex 3-like (DTX3L) is a member of the Deltex family of proteins. Initially identified as a B-lymphoma and BAL-associated protein, DTX3L is an E3 ligase that regulates subcellular localization of its partner protein, BAL, by a dynamic nucleocytoplasmic trafficking mechanism. Unlike other members of the Deltex family of proteins, DTX3L lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex proteins, and instead contains other unique N-terminal domains. The C-terminal domains are, however, homologous with other members of the Deltex family of proteins; these include a RING domain and a previously unidentified C-terminal domain. In this study, we report the high-resolution crystal structure of this previously uncharacterized C-terminal domain of human DTX3L, which we term the Deltex C-terminal domain.

PubMed: 22411408
DOI: 10.1002/prot.24054

Experimental method

X-RAY DIFFRACTION (1.7 Å)