Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-l-methionine transferase protein TehB from Escherichia coli

被引：4

作者：

Choudhury, Hassanul Ghani ^{[2
]}

Beis, Konstantinos ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, London SW7 2AZ, England

[2] Diamond Light Source, Membrane Prot Lab, Chilton OX11 0DF, Oxon, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷

关键词：

tellurite; methyltransferases; S-adenosyl-l-methionine; sinefungin; seeding; ADENOSYLMETHIONINE; METHYLTRANSFERASE; DETERMINANT; EXPRESSION; REDUCTION; SYSTEM;

D O I：

10.1107/S1744309110036043

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

TehB is an S-adenosyl-l-methionine (SAM) dependent methyltransferase that detoxifies tellurite in bacteria. The Escherichia coli TehB protein was purified and crystallized in the presence of both SAM and sinefungin. The TehB-SAM and TehB-sinefungin crystals both diffracted X-rays to 1.9 A resolution. The TehB-SAM crystals belonged to space group C2, with unit-cell parameters a = 60.0, b = 56.1, c = 130.6 A, beta = 97.9 degrees. The TehB-sinefungin crystals belonged to space group P2(1), with unit-cell parameters a = 59.1, b = 55.5, c = 129.7 A, beta = 95.9 degrees.

引用

页码：1496 / 1499

页数：4

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