6OP8
S. pombe Ubc7/U7BR complex
Summary for 6OP8
| Entry DOI | 10.2210/pdb6op8/pdb |
| Descriptor | Ubiquitin-conjugating enzyme E2-18 kDa, CUE domain-containing protein 4, mitochondrial, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | ubl conjugation pathway, endoplasmic reticulum-associated degradation, ligase, ligase-protein binding complex, ligase/protein binding |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 27131.01 |
| Authors | Hann, Z.S.,Lima, C.D. (deposition date: 2019-04-24, release date: 2019-08-07, Last modification date: 2023-10-11) |
| Primary citation | Hann, Z.S.,Metzger, M.B.,Weissman, A.M.,Lima, C.D. Crystal structure of the Schizosaccharomyces pombe U7BR E2-binding region in complex with Ubc7. Acta Crystallogr.,Sect.F, 75:552-560, 2019 Cited by PubMed Abstract: Endoplasmic reticulum (ER)-associated degradation (ERAD) is a protein quality-control pathway in eukaryotes in which misfolded ER proteins are polyubiquitylated, extracted and ultimately degraded by the proteasome. This process involves ER membrane-embedded ubiquitin E2 and E3 enzymes, as well as a soluble E2 enzyme (Ubc7 in Saccharomyces cerevisiae and UBE2G2 in mammals). E2-binding regions (E2BRs) that recruit these soluble ERAD E2s to the ER have been identified in humans and S. cerevisiae, and structures of E2-E2BR complexes from both species have been determined. In addition to sequence and structural differences between the human and S. cerevisiae E2BRs, the binding of E2BRs also elicits different biochemical outcomes with respect to E2 charging by E1 and E2 discharge. Here, the Schizosaccharomyces pombe E2BR was identified and purified with Ubc7 to resolve a 1.7 Å resolution co-crystal structure of the E2BR in complex with Ubc7. The S. pombe E2BR binds to the back side of the E2 as an α-helix and, while differences exist, it exhibits greater similarity to the human E2BR. Structure-based sequence alignments reveal differences and conserved elements among these species. Structural comparisons and biochemistry reveal that the S. pombe E2BR presents a steric impediment to E1 binding and inhibits E1-mediated charging, respectively. PubMed: 31397327DOI: 10.1107/S2053230X19009786 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.703 Å) |
Structure validation
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