Crystallization and preliminary X-ray analysis of AlgS, a bacterial ATP-binding cassette (ABC) protein specific to macromolecule import

被引：9

作者：

Mishima, Y ^{[1
]}

Momma, K ^{[1
]}

Hashimoto, W ^{[1
]}

Mikami, B ^{[1
]}

Murata, K ^{[1
]}

机构：

[1] Kyoto Univ, Food Sci Res Inst, Kyoto 6110011, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S090744490100525X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Sphingomonas sp. A1 possesses a macromolecule (alginate; average molecular size 25 700 Da) uptake system mediated by a novel pit-dependent ABC transporter. In this system, AlgS (363 amino-acid residues; 40 kDa) functions as an ATPase and provides energy for the translocation of high molecular-weight alginate across the cytoplasmic membrane. Hexahistidine-tagged AlgS of Sphingomonas sp. A1 was overexpressed in Escherichia coli and crystallized by means of the hanging-drop vapour-diffusion method with ammonium dihydrogen monophosphate as the precipitant. Preliminary X-ray analysis of the resultant crystals was performed; they belonged to the monoclinic space group P2(1) and had unit-cell parameters a = 57.4, b = 92.7, c = 65.8 Angstrom, beta = 102.3 degrees. X-ray diffraction data to 3.2 Angstrom have been collected from the native crystal.

引用

页码：884 / 885

页数：2

共 11 条

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[2] Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis [J].