Cloning, purification and preliminary crystallographic analysis of cobalamin methyltransferases from Rhodobacter capsulatus

被引:2
作者
Seyedarabi, Arefeh [1 ]
Hutchison, Thomas [1 ]
To, Teng Teng [1 ]
Deery, Evelyne [2 ]
Brindley, Amanda [2 ]
Warren, Martin J. [2 ]
Pickersgill, Richard W. [1 ]
机构
[1] Queen Mary Univ London, Sch Biol & Chem Sci, London E1 4NS, England
[2] Univ Kent, Sch Biosci, Ctr Mol Proc, Canterbury CT2 7NJ, Kent, England
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
基金
英国生物技术与生命科学研究理事会;
关键词
cobalamin methyltransferases; CobJ; CobM; CobF; CobL; Rhodobacter capsulatus; DATA QUALITY; BIOSYNTHESIS; ENZYME; CBIL;
D O I
10.1107/S1744309110042910
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Of the 30 biosynthetic steps necessary for the production of cobalamin (vitamin B-12), eight involve the addition of S-adenosylmethionine-derived methyl groups to the tetrapyrrole framework. These eight methyl additions are catalysed by six canonical methyltransferase domains and one noncanonical methyltransferase domain. Recombinant forms of four methyltransferases from Rhodobacter capsulatus, CobJ, CobM, CobF and CobL, and of the C-terminal noncanonical domain of CobL (CobL-C) have been crystallized, some in more than one crystal form. Most of the crystals diffracted to beyond 2.5 A resolution and all are suitable for structure determination. Crystals of CobM and CobJ, which are involved in ring contraction, and of CobL, which is involved in two methylations and decarboxylation, are reported for the first time.
引用
收藏
页码:1652 / 1656
页数:5
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