3K1L
Crystal Structure of FANCL
Summary for 3K1L
Entry DOI | 10.2210/pdb3k1l/pdb |
Related PRD ID | PRD_900001 |
Descriptor | Fancl, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ZINC ION, ... (6 entities in total) |
Functional Keywords | ubc, ring, rwd, ligase |
Biological source | Drosophila melanogaster (Fruit fly) |
Total number of polymer chains | 2 |
Total formula weight | 91633.88 |
Authors | Cole, A.R.,Walden, H. (deposition date: 2009-09-28, release date: 2010-02-16, Last modification date: 2024-03-20) |
Primary citation | Cole, A.R.,Lewis, L.P.C.,Walden, H. The structure of the catalytic subunit FANCL of the Fanconi anemia core complex Nat.Struct.Mol.Biol., 17:294-298, 2010 Cited by PubMed Abstract: The Fanconi anemia (FA) pathway is activated in response to DNA damage, leading to monoubiquitination of the substrates FANCI and FANCD2 by the FA core complex. Here we report the crystal structure of FANCL, the catalytic subunit of the FA core complex, at 3.2 A. The structure reveals an architecture fundamentally different from previous sequence-based predictions. The molecule is composed of an N-terminal E2-like fold, which we term the ELF domain, a novel double-RWD (DRWD) domain, and a C-terminal really interesting new gene (RING) domain predicted to facilitate E2 binding. Binding assays show that the DRWD domain, but not the ELF domain, is responsible for substrate binding. PubMed: 20154706DOI: 10.1038/nsmb.1759 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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