Structural organization of FtsB, a transmembrane protein of the bacterial divisome
| Autor: | Ivan Rayment, Alessandro Senes, Ambalika S. Khadria, Loren M. LaPointe, Keenan C. Taylor, Sabareesh Subramaniam |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Protein Conformation Glutamine Recombinant Fusion Proteins Molecular Sequence Data Cell Cycle Proteins Biology Crystallography X-Ray Biochemistry Article Escherichia coli Point Mutation Amino Acid Sequence Integral membrane protein Conserved Sequence Coiled coil Circular Dichroism Escherichia coli Proteins Mutagenesis Membrane Proteins Hydrogen Bonding Periplasmic space Transmembrane protein Protein Structure Tertiary Transmembrane domain Membrane protein Periplasm Biophysics Protein Multimerization Linker |
| Zdroj: | Biochemistry. 52(15) |
| ISSN: | 1520-4995 |
| Popis: | We report the first structural analysis of an integral membrane protein of the bacterial divisome. FtsB is a single-pass membrane protein with a periplasmic coiled coil. Its heterologous association with its partner FtsL represents an essential event for the recruitment of the late components to the division site. Using a combination of mutagenesis, computational modeling, and X-ray crystallography, we determined that FtsB self-associates, and we investigated its structural organization. We found that the transmembrane domain of FtsB homo-oligomerizes through an evolutionarily conserved interaction interface where a polar residue (Gln 16) plays a critical role through the formation of an interhelical hydrogen bond. The crystal structure of the periplasmic domain, solved as a fusion with Gp7, shows that 30 juxta-membrane amino acids of FtsB form a canonical coiled coil. The presence of conserved Gly residue in the linker region suggests that flexibility between the transmembrane and coiled coil domains is functionally important. We hypothesize that the transmembrane helices of FtsB form a stable dimeric core for its association with FtsL into a higher-order oligomer and that FtsL is required to stabilize the periplasmic domain of FtsB, leading to the formation of a complex that is competent for binding to FtsQ, and to their consequent recruitment to the divisome. The study provides an experimentally validated structural model and identifies point mutations that disrupt association, thereby establishing important groundwork for the functional characterization of FtsB in vivo. |
| Databáze: | OpenAIRE |
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