6MW7
Crystal structure of ATPase module of SMCHD1 bound to ATP
Summary for 6MW7
| Entry DOI | 10.2210/pdb6mw7/pdb |
| Descriptor | Structural maintenance of chromosomes flexible hinge domain-containing protein 1, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | ghkl-atpase, epigenetic repressor, bosma arhinia microphthalmia, fascioscapulohumeral muscular dystrophy type 2, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 263231.01 |
| Authors | Pedersen, L.C.,Inoue, K.,Kim, S.,Perera, L.,Shaw, N.D. (deposition date: 2018-10-29, release date: 2019-09-11, Last modification date: 2024-10-09) |
| Primary citation | Pedersen, L.C.,Inoue, K.,Kim, S.,Perera, L.,Shaw, N.D. A ubiquitin-like domain is required for stabilizing the N-terminal ATPase module of human SMCHD1. Commun Biol, 2:255-255, 2019 Cited by PubMed Abstract: Variants in the gene , which encodes an epigenetic repressor, have been linked to both congenital arhinia and a late-onset form of muscular dystrophy called facioscapulohumeral muscular dystrophy type 2 (FSHD2). This suggests that SMCHD1 has a diversity of functions in both developmental time and space. The C-terminal end of SMCHD1 contains an SMC-hinge domain which mediates homodimerization and chromatin association, whereas the molecular architecture of the N-terminal region, which harbors the GHKL-ATPase domain, is not well understood. We present the crystal structure of the human SMCHD1 N-terminal ATPase module bound to ATP as a functional dimer. The dimer is stabilized by a novel N-terminal ubiquitin-like fold and by a downstream transducer domain. While disease variants map to what appear to be critical interdomain/intermolecular interfaces, only the FSHD2-specific mutant constructs we tested consistently abolish ATPase activity and/or dimerization. These data suggest that the full functional profile of SMCHD1 has yet to be determined. PubMed: 31312724DOI: 10.1038/s42003-019-0499-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.194 Å) |
Structure validation
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