TY  - JOUR
N1  - Copyright of this article belongs to Elsevier Science.
ID  - open1927
UR  - http://dx.doi.org/10.1016/j.jsb.2016.08.004
IS  - 3
A1  - Acharya, Giriraj
A1  - Kaur, Gurmeet
A1  - Subramanian, Srikrishna
Y1  - 2016///
N2  - Domain/segment swapping is an exchange of equivalent secondary structure element(s) among two or more protein domains resulting in the reconstitution of the original fold while simultaneously causing oligomerization. Here we report an example of the outer membrane factor docking region of the Acr_tran family (PF00873) resistance-nodulation-cell division pump, in which a swapped, misfolded state, of the ferredoxin-like fold of the DN and DC domains, effectuates oligomerization. The atypical segment swap and the associated displacement of a region of the ferredoxin-like fold leads to a topology that is distinct from the original fold. To our knowledge, such segment swaps and associated fold change are rare. This exemplifies the role of functional constraints including oligomerization that determine the interplay between sequence and the three-dimensional structure of proteins.
JF  - Journal of Structural Biology
VL  - 196
SN  - 10478477
TI  - An atypical segment swap in the DN and DC domains of the Acr_tran family resistance-nodulation-cell division pump
SP  - 358
EP  - 363
ER  -