Crystallization and preliminary X-ray analysis of alginate importer from Sphingomonas sp A1

被引:1
作者
Maruyama, Yukie [1 ]
Itoh, Takafumi [1 ]
Nishitani, Yu [1 ]
Mikami, Bunzo [2 ]
Hashimoto, Wataru [1 ]
Murata, Kousaku [1 ]
机构
[1] Kyoto Univ, Grad Sch Agr, Div Food Sci & Biotechnol, Lab Basic & Appl Mol Biotechnol, Kyoto 6110011, Japan
[2] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Lab Appl Struct Biol, Kyoto 6110011, Japan
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷
关键词
alginate importer; AlgQ2; Sphingomonas sp; A1; MACROMOLECULE (ALGINATE)-BINDING PROTEIN; CRYSTAL-STRUCTURE; CELL-SURFACE; TRANSPORTER; RESOLUTION; MECHANISM; SYSTEM; ALGQ2;
D O I
10.1107/S1744309112001893
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Sphingomonas sp. A1 directly incorporates alginate polysaccharides through a 'superchannel' comprising a pit on the cell surface, alginate-binding proteins in the periplasm and an ABC transporter (alginate importer) in the inner membrane. Alginate importer, consisting of four subunits, AlgM1, AlgM2 and two molecules of AlgS, was crystallized in the presence of the binding protein AlgQ2. Preliminary X-ray analysis showed that the crystal diffracted to 3.3 angstrom resolution and belonged to space group P212121, with unit-cell parameters a = 72.5, b = 136.8, c = 273.3 angstrom, suggesting the presence of one complex in the asymmetric unit.
引用
收藏
页码:317 / 320
页数:4
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