Tracing the structural evolution of eukaryotic ATP binding cassette transporter superfamily

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Tracing the structural evolution of eukaryotic ATP binding cassette transporter superfamily

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Title: Tracing the structural evolution of eukaryotic ATP binding cassette transporter superfamily
Author: Xiong, Jie; Feng, Jinmei; Yuan, Dongxia; Zhou, Jun; Miao, Wei

Note: Order does not necessarily reflect citation order of authors.

Citation: Xiong, Jie, Jinmei Feng, Dongxia Yuan, Jun Zhou, and Wei Miao. 2015. “Tracing the structural evolution of eukaryotic ATP binding cassette transporter superfamily.” Scientific Reports 5 (1): 16724. doi:10.1038/srep16724. http://dx.doi.org/10.1038/srep16724.
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Abstract: The ATP binding cassette (ABC) transporters superfamily is one of the largest classes of membrane proteins. The core of the ABC transporter protein is composed of transmembrane domains (TMDs) and nucleotide binding domains (NBD). Eukaryotes ABC transporters are classified into seven main families (ABCA to ABCG) based on sequence similarity and domain organizations. With different domain number and domain organizations, eukaryote ABC transporters show diverse structures: the single structure (NBD or TMD), the ABC2 structure (NBD-NBD), the half structure (TMD-NBD or NBD-TMD) and the full structure (TMD-NBD-TMD-NBD or NBD-TMD-NBD-TMD). However, studies on how various ABC transporter gene structures evolved is still absent. Therefore, in this study, we comprehensively investigated the structural evolution of eukaryotic ABC transporters. The seven eukaryote ABC transporter families (A to G) fell into three groups: A&G group, B,C&D group and E&F group. There were at least four times the number of NBD and TMD fusion events in the origin of the half structure transporter. Two fusion modes were found in the full and ABC2 structure origination. Based on these findings, we present a putative structural evolutionary path of eukaryote ABC transporters that will increase our understanding on their origin, divergence and function.
Published Version: doi:10.1038/srep16724
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4649718/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:23845332
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