Isaacson, Rivka L.; Pye, Valerie E.; Simpson, Peter; Meyer, Hemmo; Zhang, Xiaodong; Freemont, Paul S.; Matthews, Steve:

Detailed structural insights into the p97-Npl4-Ufd1 interface

In: The journal of biological chemistry : JBC, Jg. 282 (2007) ; Nr. 29, S. 21361-21369
ISSN: 0021-9258
Zeitschriftenaufsatz / Fach: Biologie
Fakultät für Biologie » Chemische Biologie
The AAA ATPase, p97, achieves its versatility through binding to a wide
   range of cofactor proteins that adapt it to different cellular
   functions. The heterodimer UN (comprising Ufd1 and Npl4) is an adaptor
   complex that recruits p97 for numerous tasks, many of which involve the
   ubiquitin pathway. Insights into the structural specificity of p97 for
   its UN adaptor are currently negligible. Here, we present the solution
   structure of the Npl4 "ubiquitin-like" domain (UBD), which adopts a
   beta-grasp fold with a 3(10) helical insert. Moreover we performed a
   chemical shift perturbation analysis of its binding surface with the p97
   N domain. We assigned the backbone amides of the p97 N domain and probed
   both its reciprocal binding surface with Npl4 UBD and its interaction
   with the p97-binding region of Ufd1. NMR data recorded on a 400-kDa
   full-length UN-hexamer p97 complex reveals an identical mode of
   interaction. We calculated a structural model for the p97 N-Npl4 UBD
   complex, and a comparison with the p97-p47 adaptor complex reveals
   subtle differences in p97 adaptor recognition and specificity.

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