Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes

被引：11

作者：

Keller, Sascha

Pojer, Florence

Heide, Lutz

Lawson, David M. ^{[1
]}

机构：

[1] John Innes Ctr Plant Sci Res, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England

[2] Univ Tubingen, D-72076 Tubingen, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷

关键词：

D O I：

10.1107/S1744309106042527

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Crystals of recombinant CloQ (subunit MW = 35 626 Da; 324 amino acids), an aromatic prenyltransferase from Streptomyces roseochromogenes, were grown by vapour diffusion. The protein crystallizes in space group I4(1)22, with unit-cell parameters a = b = 135.19, c = 98.13 angstrom. Native data from a single crystal were recorded to a resolution of 2.2 angstrom in-house. Preliminary analysis of these data indicated that the asymmetric unit corresponds to a monomer, giving an estimated solvent content of 60.6%. CloQ is involved in the biosynthesis of the aminocoumarin antibiotic clorobiocin, which targets the essential bacterial enzyme DNA gyrase.

引用

页码：1153 / 1155

页数：3

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