Crystal structure of S-adenosylmethionine synthetase
| Autor: | Shintaro Misaki, Shigehiro Kamitori, George D. Markham, Fusao Takusagawa |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_classification
Binding Sites Multiple isomorphous replacement biology Stereochemistry Protein Conformation Protein subunit Dimer Molecular Sequence Data Active site Cell Biology Crystal structure Methionine Adenosyltransferase Crystallography X-Ray Biochemistry Divalent chemistry.chemical_compound Crystallography chemistry biology.protein Escherichia coli Transferase Amino Acid Sequence Molecular Biology Derivative (chemistry) |
| Zdroj: | The Journal of biological chemistry. 271(1) |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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