Crystallization and preliminary crystallographic analysis of the C-terminal domain of MamM, a magnetosome-associated protein from Magnetospirillum gryphiswaldense MSR-1

被引:12
|
作者
Zeytuni, Natalie
Offer, Tal
Davidov, Geula
Zarivach, Raz [1 ]
机构
[1] Ben Gurion Univ Negev, Dept Life Sci, IL-84105 Beer Sheva, Israel
关键词
MamM; magnetosome-associated proteins; Magnetospirillum gryphiswaldense MSR-1; DIFFUSION FACILITATOR FAMILY; MAGNETOTACTIC BACTERIA; MOLECULAR-MECHANISMS; CRYSTAL; BIOMINERALIZATION; MEMBRANE; GENES; FIEF;
D O I
10.1107/S1744309112025638
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
MamM is a unique magnetosome-associated protein that shares substantial homology with cation diffusion facilitator (CDF) proteins, a group of heavy-metal-ion efflux transporters that participate in metal-ion homeostasis in all domains of life. Magnetotactic bacteria utilize CDF proteins in iron-oxide biomineralization and in magnetosome formation. Here, the crystallization and preliminary X-ray analysis of recombinant Magnetospirillum gryphiswaldense MamM is reported. The C-terminal domain of MamM was crystallized in the orthorhombic space group C2221, with unit-cell parameters a = 37.1, b = 94.0, c=53.3 angstrom. X-ray diffraction data were collected to a resolution of 2.0 angstrom.
引用
收藏
页码:927 / 930
页数:4
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