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ABC转运蛋白的结构多样性。

Structural diversity of ABC transporters.

作者信息

ter Beek Josy, Guskov Albert, Slotboom Dirk Jan

机构信息

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, Netherlands.

出版信息

J Gen Physiol. 2014 Apr;143(4):419-35. doi: 10.1085/jgp.201411164. Epub 2014 Mar 17.

DOI:10.1085/jgp.201411164
PMID:24638992
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3971661/
Abstract

ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.

摘要

ATP结合盒（ABC）转运蛋白构成了一个庞大的ATP依赖性蛋白质复合物超家族，介导各种底物跨膜运输。目前已获得的14种ABC转运蛋白结构极大地推动了我们对其运输机制的深入了解，并揭示了巨大的结构多样性。尽管在所有ABC转运蛋白中，水解ATP的结构域在结构上相关，但底物转运的膜嵌入结构域采用了四种不同的不相关折叠方式。在此，我们综述ABC转运蛋白的结构特征，并讨论这种结构多样性对机制多样性的影响。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/60d8cb3235af/JGP_201411164_Fig10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/d4c3c2847e5c/JGP_201411164_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/8e0fb3264da2/JGP_201411164_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/0b009e2b1fbd/JGP_201411164_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/9c2829c61a57/JGP_201411164_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/e0c716cf62f4/JGP_201411164_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/df4b9752c9b5/JGP_201411164_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/f4d97d0e2f9f/JGP_201411164_Fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/d9b5cfd6ec38/JGP_201411164_Fig8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/18000d54e158/JGP_201411164_Fig9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/60d8cb3235af/JGP_201411164_Fig10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/d4c3c2847e5c/JGP_201411164_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/8e0fb3264da2/JGP_201411164_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/0b009e2b1fbd/JGP_201411164_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/9c2829c61a57/JGP_201411164_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/e0c716cf62f4/JGP_201411164_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/df4b9752c9b5/JGP_201411164_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/f4d97d0e2f9f/JGP_201411164_Fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/d9b5cfd6ec38/JGP_201411164_Fig8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/18000d54e158/JGP_201411164_Fig9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08f/3971661/60d8cb3235af/JGP_201411164_Fig10.jpg

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