8jzg

C. glutamicum S-adenosylmethionine synthase co-crystallized with Adenosine, triphosphate, and SAM

spinqualitylabelsall models 8jzg, resolution 2.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8jzg is a 4 chain structure with sequence from Corynebacterium glutamicum ATCC 13032. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.39Å Ligands: 3PO, ADN, GOL, K, MG, POP, SAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function METK_CORGL Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.[HAMAP-Rule:MF_00086] Publication Abstract from PubMed 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 Corynebacterium glutamicum (CgMetK). Results showed that CgMetK 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 CgMetK(E68A) variant was developed that exhibited an almost complete release of inhibition by SAM with rather enhanced enzyme activity. The crystal structure of the CgMetK(E68A) 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. Structural and Biochemical Studies on Product Inhibition of S-Adenosylmethionine Synthetase from Corynebacterium glutamicum.,Lee S, Kim S, Kim IK, Kim KJ J Agric Food Chem. 2023 Oct 16. doi: 10.1021/acs.jafc.3c05180. PMID:37846083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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