TY - JOUR
T1 - Cloning, purification and preliminary crystallographic analysis of cobalamin methyltransferases from Rhodobacter capsulatus
AU - Seyedarabi, Arefeh
AU - Hutchison, Thomas
AU - To, Teng Teng
AU - Deery, Evelyne
AU - Brindley, Amanda
AU - Warren, Martin J.
AU - Pickersgill, Richard W.
PY - 2010/12
Y1 - 2010/12
N2 - 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.
AB - 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.
KW - cobalamin methyltransferases
KW - CobF
KW - CobJ
KW - CobL
KW - CobM
KW - Rhodobacter capsulatus
UR - http://www.scopus.com/inward/record.url?scp=78650109996&partnerID=8YFLogxK
U2 - 10.1107/S1744309110042910
DO - 10.1107/S1744309110042910
M3 - Article
C2 - 21139217
AN - SCOPUS:78650109996
VL - 66
SP - 1652
EP - 1656
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
SN - 1744-3091
IS - 12
ER -