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Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate 189
Ferrer, J.L.; Ravanel, S.; Robert, M.; Dumas, R..
Cobalamin-independent methionine synthase (MetE) catalyzes the synthesis of methionine by a direct transfer of the methyl group of N5-methyltetrahydrofolate (CH3-H4PteGlun) to the sulfur atom of homocysteine (Hcy). We report here the first crystal structure of this metalloenzyme under different forms, free or complexed with the Hcy and folate substrates. The Arabidopsis thaliana MetE (AtMetE) crystals reveal a monomeric structure built by two (βα)8 barrels making a deep groove at their interface. The active site is located at the surface of the C-terminal domain, facing the large interdomain cleft. Inside the active site, His647, Cys649, and Cys733 are involved in zinc coordination, whereas Asp605, Ile437, and Ser439 interact with Hcy. Opposite the...
Tipo: Journal Article Palavras-chave: ARABIDOPSIS THALIANA; STRUCTURE TRIDIMENSIONNELLE; SITE ACTIF; HOMOCYSTEINE; FOLATE; SITE DE LIAISON; ZINC; METHIONINE.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0500031912109810&uri=/notices/prodinra1/2010/11/
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