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来自詹氏甲烷球菌 A1AOATP 合酶亚基 H 的卷曲螺旋域中二硫键的连接以及 C 端片段 H(85-104)的 NMR 结构。

Disulfide linkage in the coiled-coil domain of subunit H of A1AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H(85-104).

机构信息

School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore.

出版信息

FEBS Lett. 2010 Feb 19;584(4):713-8. doi: 10.1016/j.febslet.2009.12.024. Epub 2009 Dec 22.

DOI:10.1016/j.febslet.2009.12.024
PMID:20026332
Abstract

The C-terminal residues 98-104 are important for structure stability of subunit H of A(1)A(O) ATP synthases as well as its interaction with subunit A. Here we determined the structure of the segment H(85-104) of H from Methanocaldococcus jannaschii, showing a helix between residues Lys90 to Glu100 and flexible tails at both ends. The helix-helix arrangement in the C-terminus was investigated by exchange of hydrophobic residues to single cysteine in mutants of the entire subunit H (H(I93C), H(L96C) and H(L98C)). Together with the surface charge distribution of H(85-104), these results shine light into the A-H assembly of this enzyme.

摘要

C 端残基 98-104 对 A(1)A(O)ATP 合酶亚基 H 的结构稳定性及其与亚基 A 的相互作用非常重要。本文测定了来自产甲烷球菌的 H 亚基的 H(85-104)片段的结构，显示赖氨酸 90 到谷氨酸 100 之间存在一个螺旋，两端为柔性尾巴。通过将整个 H 亚基（H(I93C)、H(L96C)和 H(L98C)）的疏水残基交换为单个半胱氨酸，研究了 C 端螺旋-螺旋排列。结合 H(85-104)的表面电荷分布，这些结果揭示了该酶的 A-H 组装。

相似文献

[1]
Disulfide linkage in the coiled-coil domain of subunit H of A1AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H(85-104).

FEBS Lett. 2009-12-22

[2]
Small-angle X-ray scattering reveals the solution structure of the peripheral stalk subunit H of the A1AO ATP synthase from Methanocaldococcus jannaschii and its binding to the catalytic A subunit.

Biochemistry. 2007-2-27

[3]
A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A(1)A(0) ATP synthase.

J Struct Biol. 2009-4

[4]
Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A1Ao ATP synthase.

Proteins. 2009-6

[5]
NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii.

J Bioenerg Biomembr. 2009-8

[6]
Structure of the nucleotide-binding subunit B of the energy producer A1A0 ATP synthase in complex with adenosine diphosphate.

Acta Crystallogr D Biol Crystallogr. 2008-11

[7]
NMR solution structure of subunit F of the methanogenic A1AO adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B.

Biochemistry. 2007-10-23

[8]
Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms.

Biochem J. 2009-12-14

[9]
Molecular basis for the subunit assembly of the primase from an archaeon Pyrococcus horikoshii.

FEBS J. 2007-3

[10]
Identification of critical residues of subunit H in its interaction with subunit E of the A-ATP synthase from Methanocaldococcus jannaschii.

FEBS J. 2008-4

引用本文的文献

[1]
ACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils.

Sci Rep. 2017-3-7

[2]
Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering.

J Bioenerg Biomembr. 2010-6-23

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