Hi Shane, some crystal forms of trimeric AcrB (a multi-drug resistance secondary transporter) have 3 (or 6) monomers in the ASU and these are substantially different, which suggests how the protein functions. One reference is e.g. Seeger et al. (2006) "Structural Asymmetry of AcrB Trimer Suggests a Peristaltic Pump Mechanism " Science 313, 1295-1298 DOI: 10.1126/science.1131542 (sorry for the self-plug!)
best, Kay On Mon, 27 Jan 2014 13:08:33 -0500, Shane Caldwell <shane.caldwel...@gmail.com> wrote: >Hi ccp4bb, > >I'm putting together a talk for some peers that highlights strengths and >weaknesses of structural models for the outsider. For one point, I'd like >to find some examples of proteins that show very different conformations >between different copies in the ASU. One example I know of is c-Abl (1OPL), >which crystallizes with both autoinhibited and active forms in the ASU, >with dramatically different domain organization. I'd like to find some >additional examples - can anyone suggest some other structures that have >multiple copies with large structural variations? > >Thanks in advance! > >Shane Caldwell >McGill University >
