Journal article
Insights into Ubiauitin Transfer Cascades from a Structure of a UbcH5B similar to Ubiauitin-HECTNEDD4L Complex
Molecular cell, Vol.36(6), pp.1095-1102
12/24/2009
DOI: 10.1016/j.molcel.2009.11.010
PMCID: PMC2859195
PMID: 20064473
Abstract
In E1-E2-E3 ubiquitin (Ub) conjugation cascades, the E2 first forms a transient E2 similar to Ub covalent complex and then interacts with an E3 for Ub transfer. For cascades involving E3s in the HECT class, Ub is transferred from an associated E2 to the acceptor cysteine in the HECT domain C lobe. To gain insights into this process, we determined the crystal structure of a complex between the HECT domain of NEDD4L and the E2 UbcH5B bearing a covalently linked Ub at its active site (UbcH5B similar to Ub). Noncovalent interactions between UbcH5B and the HECT N lobe and between Ub and the HECT domain C lobe lead to an overall compact structure, with the Ub C terminus sandwiched between UbcH5B and HECT domain active sites. The structure suggests a model for E2-to-HECT Ub transfer, in which interactions between a donor Ub and an acceptor domain constrain upstream and downstream enzymes for conjugation.
Details
- Title: Subtitle
- Insights into Ubiauitin Transfer Cascades from a Structure of a UbcH5B similar to Ubiauitin-HECTNEDD4L Complex
- Creators
- Hari B. Kamadurai - St. Jude Children's Research HospitalJudith Souphron - St. Jude Children's Research HospitalDaniel C. Scott - St. Jude Children's Research HospitalDavid M. Duda - St. Jude Children's Research HospitalDarcie J. Miller - St. Jude Children's Research HospitalDaniel Stringer - University of IowaRobert C. Piper - University of IowaBrenda A. Schulman - St. Jude Children's Research Hospital
- Resource Type
- Journal article
- Publication Details
- Molecular cell, Vol.36(6), pp.1095-1102
- DOI
- 10.1016/j.molcel.2009.11.010
- PMID
- 20064473
- PMCID
- PMC2859195
- NLM abbreviation
- Mol Cell
- ISSN
- 1097-2765
- eISSN
- 1097-4164
- Publisher
- Elsevier
- Number of pages
- 8
- Grant note
- R01GM077053 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS) RR-15301 / NIH NCRR; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Center for Research Resources (NCRR) P41RR015301 / NATIONAL CENTER FOR RESEARCH RESOURCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Center for Research Resources (NCRR) R01GM077053; P30CA021765 / NIH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA American Heart Association Howard Hughes Medical Institute ALSAC; American Lebanese Syrian Associated Charities (ALSAC) P30CA021765 / NATIONAL CANCER INSTITUTE; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Cancer Institute (NCI) W-31-109-Eng-38 / US DOE; United States Department of Energy (DOE)
- Language
- English
- Date published
- 12/24/2009
- Academic Unit
- Molecular Physiology and Biophysics; Medicine Administration; Internal Medicine
- Record Identifier
- 9984297596702771
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