4LE5

Structure of an Unusual S-adenosylmethionine synthetase from Campylobacter jejuni

Summary for 4LE5

• Entry DOI: 10.2210/pdb4le5/pdb
• Descriptor: S-adenosylmethionine synthetase (2 entities in total)
• Functional Keywords: rossmann fold, transferase, atp binding
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 2
• Total formula weight: 94512.94

Authors

Zano, S.P.,Pavlovsky, A.G.,Viola, R.E. (deposition date: 2013-06-25, release date: 2014-02-12, Last modification date: 2023-09-20)

Primary citation

Zano, S.P.,Pavlovsky, A.G.,Viola, R.E.
Structure of an unusual S-adenosylmethionine synthetase from Campylobacter jejuni.
Acta Crystallogr.,Sect.D, 70:442-450, 2014

PubMed Abstract: S-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.

PubMed: 24531478
DOI: 10.1107/S139900471303023X

Experimental method

X-RAY DIFFRACTION (1.7 Å)