Sandbox1qu7

Serine Chemotaxis

The intact structure of Serine Chemotaxis or can be divided into 4 domains: , , and domain. Additionally, there are methylation sites in the cytoplasmic domain. This structure also shows the membrane. Unlabeled with membrane.

Function

Motile bacteria like Escherichia coli cells are attracted to and repelled by signals in their surroundings due to transmembrane chemoreceptor proteins, i.e: their direction of movement is controlled by this mechanism. The stimulus information travels through the receptor molecule, shifting the dynamic properties of adjoining structural elements. The section of the found in the cytoplasmic membrane is a helical-bundle structure signaling molecule.

Disease and Relevance

If we can understand^[1] how the bacteria moves^[1] we might be able to make antibiotics that can target those specific control sites and prevent diseases by halting their search for attractant molecules. The chemoreceptors Escherichia coli and Salmonella typhimurium are stable and ultrasensitive molecules with coupling proteins, CheW and CheA attached at the bottom. A ligand bound can stimulate change through the kinase control model as a response. Among the 3 kinase control regulations, CheA and CheW binding is done through stable spatial clustering-leading to the YinYang Hypothesis. It proposes that strong helix packing stabilizes the receptor.

Overview of Structure and Mechanism

The section of the found in the cytoplasmic membrane is a helical-bundle structure signaling molecule.

References

1)Microbial Translocation: Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update John S. Parkinson, Gerald L. Hazelbauer, and Joseph J. Falke

2)Multidimensional Solid-State Nuclear Magnetic Resonance of a Functional Multiprotein Chemoreceptor ArrayMichael J. Harris, Jochem O. Struppe, Benjamin J. Wylie, Ann E. McDermott, and Lynmarie K. Thompson*

3)Engineered Socket Study of Signaling through a Four-Helix Bundle: Evidence for aYin-Yang Mechanism in the Kinase Control Module of the Aspartate ReceptorKalin E. Swain, Miguel A. Gonzalez, and Joseph J. Falke