Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding
| Autor: | Andrew C. Eliot, Guido Capitani, Radii M. Khomutov, Heinz Gut, Markus G. Grütter, Jack F. Kirsch |
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| Rok vydání: | 2003 |
| Předmět: |
biology
ATP synthase Protein Conformation Sulfonium Stereochemistry Sulfonium Compounds Biophysics Lyases Substrate (chemistry) Crystallography X-Ray Oxime Lyase Biochemistry Cofactor Analytical Chemistry chemistry.chemical_compound chemistry Pyridoxal Phosphate parasitic diseases biology.protein 1-aminocyclopropane-1-carboxylate synthase Molecular Biology Pyridoxal |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647:55-60 |
| ISSN: | 1570-9639 |
| Popis: | The crystal structure of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with the substrate analogue [2-(amino-oxy)ethyl](5′-deoxyadenosin-5′-yl)(methyl)sulfonium (AMA) was determined at 2.01-A resolution. The crystallographic results show that a covalent adduct (oxime) is formed between AMA (an amino-oxy analogue of the natural substrate S -adenosyl- l -methionine (SAM)) and the pyridoxal 5′-phosphate (PLP) cofactor of ACC synthase. The oxime formation is supported by spectroscopic data. The ACC synthase–AMA structure provides reliable and detailed information on the binding mode of the natural substrate of ACC synthase and complements previous structural and functional work on this enzyme. |
| Databáze: | OpenAIRE |
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