The structural basis of transferrin sequestration by transferrin-binding protein B
| Autor: | Rong-hua Yu, Trevor F. Moraes, Joenel Alcantara, Charles Calmettes, Anthony B. Schryvers |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Transferrin receptor Plasma protein binding Biology Neisseria meningitidis medicine.disease_cause Article Transferrin-Binding Protein B 03 medical and health sciences Structural Biology medicine Humans Protein Interaction Domains and Motifs Protein Structure Quaternary Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences 030306 microbiology Transferrin Molecular biology 3. Good health Transport protein Biochemistry chemistry Bacterial meningitis Glycoprotein Protein Binding |
| Zdroj: | Nature structural & molecular biology |
| ISSN: | 1545-9985 |
| Popis: | Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin during infection through a surface transferrin receptor system composed of proteins TbpA and TbpB. Here we present the crystal structures of TbpB from N. meningitidis in its apo form and in complex with human transferrin. The structure reveals how TbpB sequesters and initiates iron release from human transferrin. |
| Databáze: | OpenAIRE |
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