6H3A

Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain.

Summary for 6H3A

• Entry DOI: 10.2210/pdb6h3a/pdb
• Descriptor: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1, Transcription intermediary factor 1-beta, ZINC ION (3 entities in total)
• Functional Keywords: trim28, transcriptional co-repressor, cue domain, ubuiquitin, ligase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 143125.42

Authors

Newman, J.A.,Aitkenhead, H.,Lim, M.,Williams, H.L.,Svejstrup, J.Q.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.,Bountra, C.,Gileadi, O. (deposition date: 2018-07-17, release date: 2019-06-26, Last modification date: 2024-05-15)

Primary citation

Lim, M.,Newman, J.A.,Williams, H.L.,Masino, L.,Aitkenhead, H.,Gravard, A.E.,Gileadi, O.,Svejstrup, J.Q.
A Ubiquitin-Binding Domain that Binds a Structural Fold Distinct from that of Ubiquitin.
Structure, 27:1316-1325.e6, 2019

PubMed Abstract: Ubiquitylation, the posttranslational linkage of ubiquitin moieties to lysines in target proteins, helps regulate a myriad of biological processes. Ubiquitin, and sometimes ubiquitin-homology domains, are recognized by ubiquitin-binding domains, including CUE domains. CUE domains are thus generally thought to function by mediating interactions with ubiquitylated proteins. The chromatin remodeler, SMARCAD1, interacts with KAP1, a transcriptional corepressor. The SMARCAD1-KAP1 interaction is direct and involves the first SMARCAD1 CUE domain (CUE1) and the RBCC domain of KAP1. Here, we present a structural model of the KAP1 RBCC-SMARCAD1 CUE1 complex based on X-ray crystallography. Remarkably, CUE1, a canonical CUE domain, recognizes a cluster of exposed hydrophobic and surrounding charged/amphipathic residues on KAP1, which are presented in the context of a coiled-coil domain, not in a structure resembling ubiquitin. Together, these data suggest that CUE domains may have a wider function than simply recognizing ubiquitin and the ubiquitin-fold.

PubMed: 31204252
DOI: 10.1016/j.str.2019.05.003

Experimental method

X-RAY DIFFRACTION (5.505 Å)