Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosis

被引：8
|
作者：
Patra, Dhabaleswar [1 ]
Srikalaivani, R. [1 ]
Misra, Ashish [1 ]
Singh, D. D. [1 ]
Selvaraj, M. [1 ]
Vijayan, M. [1 ]
机构：
[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词：
bacterial lectins; Mycobacterium tuberculosis; beta-trefoil fold; sugar binding; RIBOSOME-INACTIVATING PROTEIN; CRYSTAL-STRUCTURE; RECEPTOR-BINDING; COMPLEXES; TOXIN; HEMAGGLUTININ; RECOGNITION; SPECIFICITY; REFINEMENT; INSIGHTS;
D O I：
10.1107/S1744309110042892
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
A secreted lectin, Rv1419, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized and the crystals have been characterized. This represents the first X-ray investigation of a lectin or lectin-like molecule from the pathogen. The cubic crystals contain one molecule in the asymmetric unit. Sequence comparisons indicate that the lectin has a beta-trefoil fold and belongs to a well characterized family of carbohydrate-binding modules. Structural analysis of the crystals is in progress.
引用
收藏
页码：1662 / 1665
页数：4
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