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

Seyedarabi, Arefeh, Hutchison, Thomas, To, Teng Teng, Deery, Evelyne, Brindley, Amanda, Warren, Martin J. ORCID: https://orcid.org/0000-0002-6028-6456 and Pickersgill, Richard W. (2010) Cloning, purification and preliminary crystallographic analysis of cobalamin methyltransferases from Rhodobacter capsulatus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (12). pp. 1652-1656. ISSN 1744-3091

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Abstract

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.

Item Type:	Article
Uncontrolled Keywords:	cobalamin methyltransferases,cobf,cobj,cobl,cobm,rhodobacter capsulatus,biophysics,structural biology,biochemistry,genetics,condensed matter physics ,/dk/atira/pure/subjectarea/asjc/1300/1304
Faculty \ School:	Faculty of Science
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	20 Sep 2022 15:30
Last Modified:	25 Oct 2022 00:14
URI:	https://ueaeprints.uea.ac.uk/id/eprint/88519
DOI:	10.1107/S1744309110042910

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