Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	A ubiquitin chain-feeding mechanism for BRCA1-A.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Aug 11, 2026
Authors	Andrea G Murachelli / Farid El Oualid / Titia K Sixma /
PubMed Abstract	The BRCA1-A complex is a multi-subunit, metallo-deubiquitinating enzyme (metallo-DUB) involved in genome maintenance. BRCA1-A displays strict specificity for K63-linked ubiquitin, with a strong ...The BRCA1-A complex is a multi-subunit, metallo-deubiquitinating enzyme (metallo-DUB) involved in genome maintenance. BRCA1-A displays strict specificity for K63-linked ubiquitin, with a strong preference for long chains, but the mechanistic basis for this selectivity has remained unclear. To address this, we have developed an activity-based probe that is specific for metallo-DUBs and mimics di- or polyubiquitin chains of any linkage (di- and poly-ubiquitin). We have solved cryoEM structures of BRCA1-A bound to K63-linked probe chains of various length, capturing multiple conformational and catalytic states. The structures reveal how allosteric regulation of catalysis occurs within the complex and how BRCA1-A uses auxiliary ubiquitin-binding sites to engage substrate by avidity and to trigger processive cleavage. Crucially, avidity and processivity can only apply to long polyubiquitin chains, explaining BRCA1-A's substrate preference. Together, these results establish BRCA1-A as a chain-shortening DUB specialised for trimming extended K63-linked polyubiquitin chains.
External links	Nat Commun / PubMed:42581048 / PubMed Central
Methods	EM (single particle)
Resolution	3.0 - 3.6 Å
Structure data	55038 9smn EMDB-55038, PDB-9smn: BRCA1-A complex bound to K63-polyUbATA - open form StateC StateP Method: EM (single particle) / Resolution: 3.2 Å 55039 9smp EMDB-55039, PDB-9smp: BRCA1-A complex bound to K63-polyUbATA - open form double State P Method: EM (single particle) / Resolution: 3.0 Å 55040 9smr EMDB-55040, PDB-9smr: Structure of apo BRCA1-A complex in presence of K63-oligoUbATA Method: EM (single particle) / Resolution: 3.25 Å 55041 9sms EMDB-55041, PDB-9sms: BRCA1-A complex: Ubiquitin bound to BRE at the wrist site (focused 3D class) Method: EM (single particle) / Resolution: 3.3 Å 55047 9sna EMDB-55047, PDB-9sna: BRCA1-A complex bound to K63-diUbATA - open form StateC StateP Method: EM (single particle) / Resolution: 3.2 Å EMDB-55052: Structure of open BRCA1-A complex bound to polyUbATA - focused classification on elbow Ubiquitin Method: EM (single particle) / Resolution: 3.0 Å 55053 9so9 EMDB-55053, PDB-9so9: BRCA1-A complex bound to K63-oligoUbATA - closed form StateC* Method: EM (single particle) / Resolution: 3.4 Å EMDB-55054: Structure of BRCA1-A complex bound to oligoUbATA - open form Method: EM (single particle) / Resolution: 3.2 Å EMDB-55055: Apo BRCA1-A complex in presence of K63-oligoUbATA - closed form Method: EM (single particle) / Resolution: 3.6 Å EMDB-55056: BRCA1-A complex bound to K63-polyUbATA - closed form State C* Method: EM (single particle) / Resolution: 3.4 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-HOH: WATER PDB-1jpl: GGA3 VHS domain complexed with C-terminal peptide from cation-independent mannose 6-phosphate receptor
Source	homo sapiens (human)
Keywords	METAL BINDING PROTEIN / Deubiquitinase; DNA repair; Metalloprotein; Ubiquitin chains;