期刊
STRUCTURE
卷 25, 期 6, 页码 890-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.04.013
关键词
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资金
- National Institute of General Medical Sciences [R01 GM088055]
- Francis Crick Institute
- Cancer Research UK [FC001142]
- UK Medical Research Council [FC001142]
- Wellcome Trust [FC001142]
- UW Hurd Fellowship Fund
- PHS NRSA [5T32 GM007270]
- ALSAC
- NIH [R37GM069530, P30CA021765, P41GM103403]
- Howard Hughes Medical Institute
- NIH-ORIP HEI [S10 RR029205]
- DOE [DE-AC02-06CH11357]
- MRC [MC_U117565398] Funding Source: UKRI
- Medical Research Council [MC_U117565398] Funding Source: researchfish
- The Francis Crick Institute [10142] Funding Source: researchfish
RING-between-RING (RBR) E3s contain RING1 domains that are structurally similar yet mechanistically distinct from canonical RING domains. Both types of E3 bind E2 similar to biquitin (E2 similar to Ub) via their RINGs but canonical RING E3s promote closed E2 similar to Ub conformations required for direct Ub transfer from the E2 to substrate, while RBR RING1s promote open E2 similar to Ub to favor Ub transfer to the E3 active site. This different RING/E2 similar to Ub conformation determines its direct target, which for canonical RING E3s is typically a substrate or substrate-linked Ub, but is the E3 active-site cysteine in the case of RBR-type E3s. Here we show that a short extension of HHARI RING1, namely Zn2+-loop II, not present in any RING E3s, acts as a steric wedge to disrupt closed E2 similar to Ub, providing a structural explanation for the distinctive RING1-dependent conformational restriction mechanism utilized by RBR E3s.
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