X-Ray Crystal Structure of Staphylococcus aureus FemA
| Autor: | Kimberly A. Curry, Robert L. Garlick, Jeanne C. Hagadorn, Andrea M. Ho, Ronald W. Sarver, Timothy E. Benson, Veronica T. Mutchler, Gil H. Choi, D. Bryan Prince |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Staphylococcus aureus Molecular Sequence Data Lysine Peptide Peptidoglycan Biology Crystallography X-Ray medicine.disease_cause Pentapeptide repeat multiple anomalous dispersion chemistry.chemical_compound Protein structure Bacterial Proteins Structural Biology medicine Humans Amino Acid Sequence Molecular Biology X-ray crystallography chemistry.chemical_classification Binding Sites Molecular Structure TRNA binding FemA Protein Structure Tertiary Enzyme chemistry Biochemistry tRNA binding Sequence Alignment |
| Zdroj: | Structure. 10:1107-1115 |
| ISSN: | 0969-2126 |
| Popis: | The latter stages of peptidoglycan biosynthesis in Staphylococci involve the synthesis of a pentaglycine bridge on the ϵ amino group of the pentapeptide lysine side chain. Genetic and biochemical evidence suggest that sequential addition of these glycines is catalyzed by three homologous enzymes, FemX (FmhB), FemA, and FemB. The first protein structure from this family, Staphylococcus aureus FemA, has been solved at 2.1 A resolution by X-ray crystallography. The FemA structure reveals a unique organization of several known protein folds involved in peptide and tRNA binding. The surface of the protein also reveals an L-shaped channel suitable for a peptidoglycan substrate. Analysis of the structural features of this enzyme provides clues to the mechanism of action of S. aureus FemA. |
| Databáze: | OpenAIRE |
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