Sandbox1qu7

(Difference between revisions)

==Serine Chemotaxis==

~~This is the total~~<scene name='78/782579/Cartooncylinder/2'> ~~ser~~ receptor</scene>~~but it~~ can be divided into 4 domains: <scene name='78/782579/The_periplasmic/1'>periplasmic</scene>, transmembrane, <scene name='78/782579/Hampdomain/1'>HAMP</scene> and <scene name='78/782579/Cytoplasmic_domain/1'>cytoplasmic domain</scene>. ~~This also includes the~~ <scene name='78/782579/Methylation_cites/1'>methylation cites</scene>in the cytoplasmic domain.

The whole structure of<scene name='78/782579/Cartooncylinder/2'> Ser receptor</scene> can be divided into 4 domains: <scene name='78/782579/The_periplasmic/1'>periplasmic</scene>, transmembrane, <scene name='78/782579/Hampdomain/1'>HAMP</scene> and <scene name='78/782579/Cytoplasmic_domain/1'>cytoplasmic domain</scene>. Additionally, there are<scene name='78/782579/Methylation_cites/1'>methylation cites</scene> in the cytoplasmic domain.

The<scene name='78/782579/Serreceptor/3'> Ser Receptor</scene> is a helical-bundle structure signaling molecule ~~found in the cytoplasmic membrane. The ligand binds to the top of the long alpha structures, sending a signal across the membrane into the cell proteins that bind near the bottom~~.

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<scene name='78/782579/Serreceptor/3'> Ser Receptor</scene> found in the cytoplasmic membrane is a helical-bundle structure signaling molecule.

== Disease and Relevance ==

If we can understand how the bacteria moves 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<scene name='78/782579/Serreceptor/3'> Ser Receptor</scene> found in the cytoplasmic membrane is a helical-bundle structure signaling molecule.

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

spinqualitylabelsall models

This is the whole intact Tsr Receptor with no ligand attached

This the structure of Ser Protein which is in the transmembrane domain, this forms a trimer of dimers (PDB entry 1qu7)

Drag the structure with the mouse to rotate

1 Function
2 Disease and Relevance
3 Overview of Structure and Mechanism
4 References

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 how the bacteria moves 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

From Proteopedia

Revision as of 11:17, 23 March 2018

Serine Chemotaxis

Contents

Function

Disease and Relevance

Overview of Structure and Mechanism

References

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@@ Line 1: / Line 1: @@
 ==Serine Chemotaxis==
-This is the total<scene name='78/782579/Cartooncylinder/2'> ser receptor</scene>but it can be divided into 4 domains: <scene name='78/782579/The_periplasmic/1'>periplasmic</scene>, transmembrane, <scene name='78/782579/Hampdomain/1'>HAMP</scene> and <scene name='78/782579/Cytoplasmic_domain/1'>cytoplasmic domain</scene>. This also includes the <scene name='78/782579/Methylation_cites/1'>methylation cites</scene>in the cytoplasmic domain.
+The whole structure of<scene name='78/782579/Cartooncylinder/2'> Ser receptor</scene> can be divided into 4 domains: <scene name='78/782579/The_periplasmic/1'>periplasmic</scene>, transmembrane, <scene name='78/782579/Hampdomain/1'>HAMP</scene> and <scene name='78/782579/Cytoplasmic_domain/1'>cytoplasmic domain</scene>. Additionally, there are<scene name='78/782579/Methylation_cites/1'>methylation cites</scene> in the cytoplasmic domain.
-<Structure load='Insert PDB code or filename here' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
+<Structure load='Insert PDB code or filename here' size='350' frame='true' align='right' caption='This is the whole intact  Tsr Receptor with no ligand attached' scene='Insert optional scene name here' />
 <StructureSection load='1qu7' size='350' side='right' caption='This the structure of Ser Protein which is in the transmembrane domain, this forms a trimer of dimers (PDB entry [[1qu7]])' scene=''>
 == Function ==
-The<scene name='78/782579/Serreceptor/3'> Ser Receptor</scene> is a helical-bundle structure signaling molecule found in the cytoplasmic membrane. The ligand binds to the top of the long alpha structures, sending a signal across the membrane into the cell proteins that bind near the bottom.
+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<scene name='78/782579/Serreceptor/3'> Ser Receptor</scene> found in the cytoplasmic membrane is a helical-bundle structure signaling molecule.
 == Disease and Relevance ==
+If we can understand how the bacteria moves 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.
@@ Line 14: / Line 14: @@
 == Overview of Structure and Mechanism ==
+The section of the<scene name='78/782579/Serreceptor/3'> Ser Receptor</scene> found in the cytoplasmic membrane is a helical-bundle structure signaling molecule.
 == References ==
+)Microbial Translocation: Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update
+John S. Parkinson, Gerald L. Hazelbauer, and Joseph J. Falke
+)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*
+)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
 </StructureSection>