Cloning, purification and preliminary crystallographic analysis of cobalamin methyltransferases from Rhodobacter capsulatus.
Cloning, purification and preliminary crystallographic analysis of cobalamin methyltransferases from Rhodobacter capsulatus.
复制标题
荚膜红杆菌钴胺素甲基转移酶的克隆、纯化和初步晶体学分析。
DOI:
10.1107/s1744309110042910
复制
发表时间:
2010
期刊:
影响因子:
--
通讯作者:
Seyedarabi A
中科院分区:
文献类型:
--
作者:
Seyedarabi A
Of the 30 biosynthetic steps necessary for the production of cobalamin (vitamin B12), 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 Å 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.
影响因子:
5.6
作者:
J. Vévodová;R. Graham;E. Raux;H. Schubert;D. Roper;A. Brindley;A. Ian Scott;C. Roessner;N. Stamford;M. Elizabeth Stroupe;E. Getzoff;M. Warren;K. Wilson
通讯作者:
J. Vévodová;R. Graham;E. Raux;H. Schubert;D. Roper;A. Brindley;A. Ian Scott;C. Roessner;N. Stamford;M. Elizabeth Stroupe;E. Getzoff;M. Warren;K. Wilson