8JZH

C. glutamicum S-adenosylmethionine synthase

Summary for 8JZH

• Entry DOI: 10.2210/pdb8jzh/pdb
• Descriptor: S-adenosylmethionine synthase, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• Functional Keywords: s-adenosylmethionine synthase, complex, sam, transferase
• Biological source: Corynebacterium glutamicum ATCC 13032
• Total number of polymer chains: 3
• Total formula weight: 136034.86

Authors

Lee, S.,Kim, K.J. (deposition date: 2023-07-05, release date: 2023-10-25, Last modification date: 2023-11-08)

Primary citation

Lee, S.,Kim, S.,Kim, I.K.,Kim, K.J.
Structural and Biochemical Studies on Product Inhibition of S-Adenosylmethionine Synthetase from Corynebacterium glutamicum .
J.Agric.Food Chem., 71:15692-15700, 2023

PubMed Abstract: S-Adenosylmethionine (SAM) acts as a methyl donor in living organisms, and S-adenosylmethionine synthetase (MetK) is an essential enzyme for cells, as it synthesizes SAM from methionine and adenosine triphosphate (ATP). This study determined the crystal structures of the apo form and adenosine/triphosphate complex form of MetK from (MetK). Results showed that MetK has an allosteric inhibitor binding site for the SAM product in the vicinity of the active site and is inhibited by SAM both competitively and noncompetitively. Through structure-guided protein engineering, the MetK variant was developed that exhibited an almost complete release of inhibition by SAM with rather enhanced enzyme activity. The crystal structure of the MetK variant revealed that the formation of a new hydrogen bond between Tyr66 and Glu102 by the E68A mutation disrupted the allosteric SAM binding site and also improved the protein thermal stability by strengthening the tetramerization of the enzyme.

PubMed: 37846083
DOI: 10.1021/acs.jafc.3c05180

Experimental method

X-RAY DIFFRACTION (2.2 Å)