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Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA.

Abstract：

:Despite the importance of Mg(2+) for numerous cellular activities, the mechanisms underlying its import and homeostasis are poorly understood. The CorA family is ubiquitous and is primarily responsible for Mg(2+) transport. However, the key questions-such as, the ion selectivity, the transport pathway, and the gating mechanism-have remained unanswered for this protein family. We present a 3.2 Å resolution structure of the archaeal CorA from Methanocaldococcus jannaschii, which is a unique complete structure of a CorA protein and reveals the organization of the selectivity filter, which is composed of the signature motif of this family. The structure reveals that polar residues facing the channel coordinate a partially hydrated Mg(2+) during the transport. Based on these findings, we propose a unique gating mechanism involving a helical turn upon the binding of Mg(2+) to the regulatory intracellular binding sites, and thus converting a polar ion passage into a narrow hydrophobic pore. Because the amino acids involved in the uptake, transport, and gating are all conserved within the entire CorA family, we believe this mechanism is general for the whole family including the eukaryotic homologs.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Guskov A,Nordin N,Reynaud A,Engman H,Lundbäck AK,Jong AJ,Cornvik T,Phua T,Eshaghi S

doi

10.1073/pnas.1210076109

subject

Has Abstract

pub_date

2012-11-06 00:00:00

pages

18459-64

issue

45

eissn

0027-8424

issn

1091-6490

pii

1210076109

journal_volume

109

pub_type

杂志文章

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