Ontology highlight
ABSTRACT:
SUBMITTER: Zhang N
PROVIDER: S-EPMC2748877 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Zhang Naixia N Wang Qinghua Q Ehlinger Aaron A Randles Leah L Lary Jeffrey W JW Kang Yang Y Haririnia Aydin A Storaska Andrew J AJ Cole James L JL Fushman David D Walters Kylie J KJ
Molecular cell 20090801 3
Degradation by the proteasome typically requires substrate ubiquitination. Two ubiquitin receptors exist in the proteasome, S5a/Rpn10 and Rpn13. Whereas Rpn13 has only one ubiquitin-binding surface, S5a binds ubiquitin with two independent ubiquitin-interacting motifs (UIMs). Here, we use nuclear magnetic resonance (NMR) and analytical ultracentrifugation to define at atomic level resolution how S5a binds K48-linked diubiquitin, in which K48 of one ubiquitin subunit (the "proximal" one) is coval ...[more]