4le5
Structure of an Unusual S-adenosylmethionine synthetase from Campylobacter jejuniStructure of an Unusual S-adenosylmethionine synthetase from Campylobacter jejuni
Structural highlights
Publication Abstract from PubMedS-Adenosylmethionine (AdoMet) participates in a wide range of methylation and other group-transfer reactions and also serves as the precursor for two groups of quorum-sensing molecules that function as regulators of the production of virulence factors in Gram-negative bacteria. The synthesis of AdoMet is catalyzed by AdoMet synthetases (MATs), a ubiquitous family of enzymes found in species ranging from microorganisms to mammals. The AdoMet synthetase from the bacterium Campylobacter jejuni (cjMAT) is an outlier among this homologous enzyme family, with lower sequence identity, numerous insertions and substitutions, and higher catalytic activity compared with other bacterial MATs. Alterations in the structure of this enzyme provide an explanation for its unusual dimeric quaternary structure relative to the other MATs. Taken together with several active-site substitutions, this new structure provides insights into its improved kinetic properties with alternative substrates. Structure of an unusual S-adenosylmethionine synthetase from Campylobacter jejuni.,Zano SP, Pavlovsky AG, Viola RE Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):442-50. doi:, 10.1107/S139900471303023X. Epub 2014 Jan 29. PMID:24531478[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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