Crystallization and preliminary crystallographic study of b0220, an 'ORFan' protein of unknown function from Escherichia coli

被引：4

作者：

Abergel, C ^{[1
]}

Monchois, V ^{[1
]}

Chenivesse, S ^{[1
]}

Jeudy, S ^{[1
]}

Claverie, JM ^{[1
]}

机构：

[1] AVENTIS, CNRS, UMR1889, F-13402 Marseille 20, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2000年 / 56卷

关键词：

D O I：

10.1107/S0907444900015316

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Newly sequenced microbial genomes continue to reveal up to 50% functionally uncharacterized 'anonymous' genes. A significant fraction of these anonymous ORFs does not exhibit any sequence similarity to any protein in the databases and constitutes a set of unique sequences, denoted 'ORFans'. The structure determination of ORFan proteins is both of evolutionary and functional interest. Here, the first crystallization of an Escherichia coli ORFan gene product, the 157 amino-acid b0220 protein, is reported. The crystals belong to the trigonal space group P3 or P3(1), with unit-cell parameters a = b = 47.2, c = 88.4 Angstrom. There are two molecules in the asymetric unit. Frozen crystals diffract to 1.6 Angstrom resolution using synchrotron radiation. Phasing was performed using multiwavelength anomalous dispersion (MAD) on the selenomethionine-substituted b0220 protein.

引用

页码：1694 / 1695

页数：2

共 13 条

[1] Reverse transcriptase-polymerase chain reaction validation of 25 "orphan" genes from Escherichia coli K-12 MG1655 [J].