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Discontinuous membrane helices in transport proteins and their correlation with function.

Abstract：

:Alpha-helical bundles and beta-barrel proteins represent the two basic types of architecture known for integral membrane proteins. Irregular structural motifs have been revealed with the growing number of structures determined. "Discontinuous" helices are present in membrane proteins that actively transport ions. In the Ca(2+)-ATPase, a primary active transporter, and in the secondary transporters NhaA, LeuT(Aa), ClC H(+)/Cl(-) exchanger and Glt(Ph), the helical structure of two membrane segments is interrupted and the interjacent polypeptide chain forms an extended peptide. The discontinuous helices are integrated in the membrane either as transmembrane-spanning or hairpin-type segments. In addition, the secondary transporters have inverted internal duplication domains, which are only weakly correlated with their amino acid sequence. The symmetry comprises either parts of or the complete molecule, but always includes the discontinuous helices. The helix-peptide-helix motif is correlated with the ion translocation function. The extended peptides with their backbone atoms, the helix termini and the polar/charged amino acid residues in close vicinity provide the basis for ion recognition, binding and translocation.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Screpanti E,Hunte C

doi

10.1016/j.jsb.2007.01.011

subject

Has Abstract

pub_date

2007-08-01 00:00:00

pages

261-7

issue

2

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(07)00031-7

journal_volume

159

pub_type

杂志文章,评审

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