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

  

Authors:	Huang, L.; Hung, L.; Odell, M.; Yokota, H.; Kim, R.; Kim, S. H.
Article Title:	Structure-based experimental confirmation of biochemical function to a methyltransferase, MJ0882, from hyperthermophile Methanococcus jannaschii
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.
Keywords:	nonhuman; protein conformation; protein motif; protein binding; structure-activity relationship; bacteria (microorganisms); methyltransferase; bacterial proteins; amino acid sequence; molecular sequence data; sequence homology, amino acid; recombinant fusion proteins; s-adenosylhomocysteine; sequence alignment; binding protein; binding site; models, molecular; crystallography, x-ray; mutagenesis, site-directed; sequence homology; enzyme structure; nad; amino acid motifs; structural genomics; x-ray crystallography; s-adenosylmethionine; open reading frame; s adenosylmethionine; open reading frames; thermophilic bacterium; priority journal; article; methanococcus jannaschii; rossman fold; methanococcus; site-specific dna-methyltransferase (adenine-specific); methanocaldococcus jannaschii
Journal Title:	Journal of Structural and Functional Genomics
Volume:	2
Issue:	3
ISSN:	1345-711X
Publisher:	Springer
Date Published:	2002-09-01
Start Page:	121
End Page:	127
Language:	English
DOI:	10.1023/a:1021279113558
PUBMED:	12836702
PROVIDER:	scopus
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-0036906006&partnerID=40&md5=2257c042b2ed4998dd672aa8f4f320c2
Notes:	Export Date: 14 November 2014 -- Source: Scopus

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