Structure-based experimental confirmation of biochemical function to a methyltransferase, MJ0882, from hyperthermophile Methanococcus jannaschii

Huang, L., Hung, L., Odell, M., Yokota, H., Kim, R. and Kim, S.H. 2002. Structure-based experimental confirmation of biochemical function to a methyltransferase, MJ0882, from hyperthermophile Methanococcus jannaschii. Journal of Structural and Functional Genomics. 2 (3), pp. 121-127.

TitleStructure-based experimental confirmation of biochemical function to a methyltransferase, MJ0882, from hyperthermophile Methanococcus jannaschii
AuthorsHuang, L., Hung, L., Odell, M., Yokota, H., Kim, R. and Kim, S.H.
Abstract

We have determined the three-dimensional (3-D) structure of protein MJ0882, which derives from a hypothetical open reading frame in the genome of the hyperthermophile Methanococcus jannaschii. The 3-D fold of MJ0882 at 1.8 Å highly resembles that of a methyltransferase, despite limited sequence similarity to any confirmed methyltransferase. The structure has an S-adenosylmethionine (AdoMet) binding pocket surrounded by motifs with similarities to those commonly found among AdoMet binding proteins. Preliminary biochemical experiments show that MJ0882 specifically binds to AdoMet, which is the essential co-factor for methyltransferases.

JournalJournal of Structural and Functional Genomics
Journal citation2 (3), pp. 121-127
ISSN1345-711X
YearSep 2002
Digital Object Identifier (DOI)doi:10.1023/A:1021279113558
Publication dates
PublishedSep 2002

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