NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues

被引：12

作者：

Nielsen, G

Malmendal, A

Meissner, A

Moller, JV

Nielsen, NC

机构：

[1] Aarhus Univ, Interdisciplinary Nanosci Ctr, DK-8000 Aarhus C, Denmark

[2] Aarhus Univ, NMR Ctr, Dept Biol Mol, DK-8000 Aarhus C, Denmark

[3] Carlsberg Lab, Dept Chem, DK-2500 Valby, Denmark

[4] Aarhus Univ, Dept Biophys, DK-8000 Aarhus C, Denmark

来源：

FEBS LETTERS | 2003年 / 544卷 / 1-3期

关键词：

Ca2+-ATPase; fifth transmembrane segment M5; membrane protein; micelle; nuclear magnetic resonance; sarcoplasmic reticulunt; sodium dodecyl sulfate;

D O I：

10.1016/S0014-5793(03)00448-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two recent X-ray structures have tremendously increased the understanding of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and related proteins. Both structures show the fifth transmembrane span (M5) as a single continuous alpha-helix. The inherent structural and dynamic features of this span (Lys758-Glu785) were studied in isolation in sodium dodecyl sulfate (SDS) micelles using liquid-state nuclear magnetic resonance (NMR) spectroscopy. We find that a flexible region (Ile765-Asn768) is interrupting the alpha-helix. The location of the flexible region near the Ca2+ binding residues Asn768 and Glu771 suggests that together with a similar region in M6 it has a hinge function that may be important for cooperative Ca2+ binding and occlusion. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：50 / 56

页数：7

共 63 条

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