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Crystal structure of S-adenosylmethionine synthetase.

Takusagawa F, Kamitori S, Misaki S, Markham GD
J Biol Chem 271 136-47 (1996)
Related entries: 1xrb, 1xrc

Cited: 63 times
EuropePMC logo PMID: 8550549

Abstract

The structure of S-adenosylmethionine synthetase (MAT, ATP:L-methionine S-adenosyltransferase, EC 2.5.1.6.) from Escherichia coli has been determined at 3.0 A resolution by multiple isomorphous replacement using a uranium derivative and the selenomethionine form of the enzyme (SeMAT). The SeMAT data (9 selenomethionine residues out of 383 amino acid residues) have been found to have a sufficient phasing power to determine the structure of the 42,000 molecular weight protein by combining them with the other heavy atom derivative data (multiple isomorphous replacement). The enzyme consists of four identical subunits; two subunits form a spherical tight dimer, and pairs of these dimers form a peanut-shaped tetrameric enzyme. Each pair dimer has two active sites which are located between the subunits. Each subunit consists of three domains that are related to each other by pseudo-3-fold symmetry. The essential divalent (Mg2+/Co2+) and monovalent (K+) metal ions and one of the product, Pi ions, were found in the active site from three separate structures.

Reviews - 1xra mentioned but not cited (1)

  1. Structure-function relationships in methionine adenosyltransferases. Markham GD, Pajares MA. Cell Mol Life Sci 66 636-648 (2009)

Articles - 1xra mentioned but not cited (3)

  1. Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits. Shafqat N, Muniz JR, Pilka ES, Papagrigoriou E, von Delft F, Oppermann U, Yue WW. Biochem J 452 27-36 (2013)
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Reviews citing this publication (6)

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