An atypical segment swap in the DN and DC domains of the Acr_tran family resistance-nodulation-cell division pump.

Acharya, Giriraj and Kaur, Gurmeet and Subramanian, Srikrishna (2016) An atypical segment swap in the DN and DC domains of the Acr_tran family resistance-nodulation-cell division pump. Journal of structural biology. ISSN 1095-8657 (In Press)

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Abstract

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.

Item Type: Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Uncontrolled Keywords: Domain duplication; Domain swapping; Fold change; Membrane proteins; Metamorphic proteins; RND pump
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 30 Sep 2016 05:37
Last Modified: 30 Sep 2016 05:37
URI: http://crdd.osdd.net/open/id/eprint/1849

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