Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH

Colin M. Hammond, Tom Owen-Hughes (Lead / Corresponding author), David G. Norman (Lead / Corresponding author)

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    3 Citations (Scopus)
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    Abstract

    Crystallographic and NMR approaches have provided a wealth of structural information about protein domains. However, often these domains are found as components of larger multi domain polypeptides or complexes. Orienting domains within such contexts can provide powerful new insight into their function. The combination of site specific spin labelling and Pulsed Electron Double Resonance (PELDOR) provide a means of obtaining structural measurements that can be used to generate models describing how such domains are oriented. Here we describe a pipeline for modelling the location of thio-reactive nitroxyl spin locations to engineered sties on the histone chaperone Vps75. We then use a combination of experimentally determined measurements and symmetry constraints to model the orientation in which homodimers of Vps75 associate to form homotetramers using the XPLOR-NIH platform. This provides a working example of how PELDOR measurements can be used to generate a structural model.

    Original languageEnglish
    Pages (from-to)139-153
    Number of pages15
    JournalMethods (San Diego, Calif.)
    Volume70
    Issue number2-3
    DOIs
    Publication statusPublished - Dec 2014

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