Crystal structure of S-adenosylmethionine synthetase

被引:105
作者
Takusagawa, F
Kamitori, S
Misaki, S
Markham, GD
机构
[1] UNIV KANSAS,DEPT BIOCHEM,LAWRENCE,KS 66045
[2] FOX CHASE CANC CTR,INST CANC RES,PHILADELPHIA,PA 19111
关键词
D O I
10.1074/jbc.271.1.136
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom 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, P-i ions, were found in the active site from three separate structures.
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收藏
页码:136 / 147
页数:12
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