Proteopedia - User contributions [en]

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-21T16:08:17Z

Meili Yang:

[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

<Structure load='1qu7' size='300' frame='true' align='right' caption='Cytoplasmic domain of Tsr' scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Cytoplasmic_domain_of_tsr/1' />

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

===3D structures of methyl-accepting chemotaxis protein===

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===Chemoreceptor array===

<Structure load='3ur1' size='300' frame='true' align='left' caption='A ternary complex between CheA domains P4 and P5 with CheW and with a truncated chemoreceptor.'
scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Complex/3' />

Transmembrane receptors, histidine kinases (CheA) and coupling protein (CheW) form an organized array at cell membrane. In the array, six trimers of receptor dimers combined vertically in a hexagonal lattice with CheA regulatory domains (P5) and CheW surrounded. Whereas the CheA kinase domains (P4) lie downward below the ring, the CheA dimerization domains (P3) link neighboring rings to extend the array.

===Related molecule===

[[Molecular Playground/CheA]],[[Molecular Playground/Bacterial Chemotaxis Receptors]],[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]],[[Methyl-accepting chemotaxis protein]]

===Reference===

1.Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.
2.Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells, Ariane Briege, Xiaoxiao Li and ''et.al.'', ''PNAS''.2012 Mar 6;109(10):3766-3771

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-21T02:41:23Z

Meili Yang:

[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

<Structure load='1qu7' size='300' frame='true' align='right' caption='Cytoplasmic domain of Tsr' scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Cytoplasmic_domain_of_tsr/1' />

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

===3D structures of methyl-accepting chemotaxis protein===

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===Chemoreceptor array===

[[Image:ring.png|thumb|400px|left|<b>Receptor/cheW/cheA ring</b>]]

Transmembrane receptors, histidine kinases (CheA) and coupling protein (CheW) form an organized array at cell membrane. In the array, six trimers of receptor dimers combined vertically in a hexagonal lattice with CheA regulatory domains (P5) and CheW surrounded. Whereas the CheA kinase domains (P4) lie downward below the ring, the CheA dimerization domains (P3) link neighboring rings to extend the array.

===Related molecule===

[[Molecular Playground/CheA]],[[Molecular Playground/Bacterial Chemotaxis Receptors]],[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]],[[Methyl-accepting chemotaxis protein]]

===Reference===

1.Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.
2.Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells, Ariane Briege, Xiaoxiao Li and ''et.al.'', ''PNAS''.2012 Mar 6;109(10):3766-3771

<Structure load='3ur1' size='400' frame='true' align='right' caption='A ternary complex between CheA domains P4 and P5 with CheW and with a truncated chemoreceptor.'
scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Complex/3' />

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-21T01:23:16Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

<Structure load='1qu7' size='300' frame='true' align='right' caption='Cytoplasmic domain of Tsr' scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Cytoplasmic_domain_of_tsr/1' />

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

===3D structures of methyl-accepting chemotaxis protein===

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===Chemoreceptor array===

[[Image:ring.png|thumb|400px|left|<b>Receptor/cheW/cheA ring</b>]]

<Structure load='3ur1' size='400' frame='true' caption='A ternary complex between CheA domains P4 and P5 with CheW and with a truncated chemoreceptor.' scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Complex/3'>

[[Methyl-accepting chemotaxis protein]]

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-21T01:15:51Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

<Structure load='1qu7' size='300' frame='true' align='right' caption='Cytoplasmic domain of Tsr' scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Cytoplasmic_domain_of_tsr/1' />

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

===3D structures of methyl-accepting chemotaxis protein===

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===Chemoreceptor array===

[[Image:ring.png|thumb|400px|left|<b>Receptor/cheW/cheA ring</b>]]

<Structure load='3ur1' size='400' frame='true' align='left' caption='A ternary complex between CheA domains P4 and P5 with CheW and with a truncated chemoreceptor.' scene='''Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Complex/2'' />

[[Methyl-accepting chemotaxis protein]]

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T22:13:17Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

<Structure load='1qu7' size='500' frame='true' align='right' caption='Cytoplasmic domain of Tsr' scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Cytoplasmic_domain_of_tsr/1' />

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

===3D structures of methyl-accepting chemotaxis protein===

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

[[Methyl-accepting chemotaxis protein]]
''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T22:02:21Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

===3D structures of methyl-accepting chemotaxis protein===
The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

[[Methyl-accepting chemotaxis protein]]
<Structure load='1qu7' size='500' frame='true' align='right' caption='Cytoplasmic domain of Tsr' scene='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Cytoplasmic_domain_of_tsr/1' />

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T21:51:25Z

Meili Yang: /* 3D structures of methyl-accepting chemotaxis protein */

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

===3D structures of methyl-accepting chemotaxis protein===
The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

<scene name='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Cytoplasmic_domain_of_tsr/1'>TextToBeDisplayed</scene>
[[Methyl-accepting chemotaxis protein]]

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T21:48:29Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

===3D structures of methyl-accepting chemotaxis protein===
The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

[[Methyl-accepting chemotaxis protein]]

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T21:46:25Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===3D structures of methyl-accepting chemotaxis protein===

[[Methyl-accepting chemotaxis protein]]

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T21:44:47Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

{{Clear}}

=== Cytoplasmic domain of TSR ===

{{Clear}}
<table align="right" width="300" border="0" style="background-color:#e0e0e0;"><tr><td>
<applet load='2ho9' size='[450,338]' frame='true' align='right'
caption='Cytoplasmic domain of a serine chemotaxis receptor [[1qu7]]' <scene name='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Tsr_cf/1'>TextToBeDisplayed</scene>
'>

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===3D structures of methyl-accepting chemotaxis protein===

[[Methyl-accepting chemotaxis protein]]

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T21:43:16Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----
<table align="right" width="300" border="0" style="background-color:#e0e0e0;"><tr><td>

= Chemotaxis receptors =
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

{{Clear}}

=== Cytoplasmic domain of TSR ===

{{Clear}}
<applet load='2ho9' size='[450,338]' frame='true' align='right'
caption='Cytoplasmic domain of a serine chemotaxis receptor [[1qu7]]' <scene name='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Tsr_cf/1'>TextToBeDisplayed</scene>
'>

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===3D structures of methyl-accepting chemotaxis protein===

[[Methyl-accepting chemotaxis protein]]

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2012-12-20T21:36:30Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
----
<table align="right" width="300" border="0" style="background-color:#e0e0e0;"><tr><td>
<scene name='Molecular_Playground/cytoplasmic_domain_of_a_serine_chemotaxis_receptor/Tsr_cf/1'>TextToBeDisplayed</scene>

The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

{{Clear}}

=== Cytoplasmic domain of TSR ===

{{Clear}}
<applet load='2ho9' size='[450,338]' frame='true' align='right'
caption='Cytoplasmic domain of a serine chemotaxis receptor [[1qu7]]' scene='User:Meili_Yang/sandbox_1/Tsr_cf/1'>

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

===3D structures of methyl-accepting chemotaxis protein===

[[Methyl-accepting chemotaxis protein]]

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2010-12-12T22:35:01Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].

The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

{{Clear}}

=== Cytoplasmic domain of TSR ===

{{Clear}}
<applet load='2ho9' size='[450,338]' frame='true' align='right'
caption='Cytoplasmic domain of a serine chemotaxis receptor(1qu7)' scene='User:Meili_Yang/sandbox_1/Tsr_cf/1'>

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

CBI Molecules

2010-12-10T22:02:09Z

Meili Yang:

These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].
Many of the molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground]. Follow the links below to read nontechnical descriptions in Proteopedia.

UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.

Fall 2010: New entries are due 12/10/10. Please append the designation (new Fall 2010) to your new entries. If you want to build on a previous entry, leave the earlier one intact and make a copy that you improve and mark as new. Later we will retain the new one with a merged author list.

Bhatia Lab
: '''[[Molecular Playground/Alginate]]''', David Griffin

[http://chamberslab.com/wp/ Chambers Lab]

: '''[[Molecular Playground/Glutamate Receptor]]''', Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano

Forbes Lab

: '''[[Molecular Playground/TRAIL]]''', Charley Swofford

[http://www.biochem.umass.edu/garman/index.html Garman Lab]

: '''[[Molecular Playground/Human Protective Protein Cathepsin A]]''', Yadilette Rivera-Colon

: '''[[Molecular Playground/Human PPCA]]''', Nilima Kolli

[http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]

: '''[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]''', Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy
:: Best Overall CBI Molecule 2010

[http://people.chem.umass.edu/jhardy/ Hardy Lab]

: '''[[Molecular Playground/Caspase-7 Dynamics]]'''

: '''[[Molecular Playground/Caspase-9 Regulation]]''', Kristen Huber

: '''[[Molecular Playground/Caspase-6 (new)]]''', Elih Velazquez

: '''[[Molecular Playground/Influenza A M2 transmembrane domain]]''', Samantha Nicholls

Hebert Lab

: '''[[Molecular_Playground/ERMan1]]''', Johan Sunryd

Kaltashov Lab

: '''[[Molecular Playground/Velaglucerase]]''', Adriana Kita

Knapp lab

:'''[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]''', Cristina Martin
:: Best CBI Molecule Proteopedia Page 2010

: '''[[Molecular Playground/FIH]]''', Cornelius Taabazuing, Breanne Holmes, John Hangasky

[http://www.chem.umass.edu/~cmartin/ Martin Lab]

: '''[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]''', Ankit Vahia

[http://robertsgroup.ecs.umass.edu/ Roberts Lab]

: '''[[Molecular Playground/Taxol]]''', Rohan Patil, Sarah Wilson

: '''[[Molecular Playground/Insulin]]''', Whitney Stoppel

[http://www.umass.edu/rotellogroup/ Rotello Lab]

: '''[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]''', Daniel Moyano-Marino

: '''[[Molecular Playground/Pancreatic Lipase]]''', Rui Tang

: '''[[Molecular playground/Chymotrypsin]]''', Brad

: '''[[Molecular Playground/Targeting Peptide]]''', David Solfiell

Schnarr Lab

: '''[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]''', Tsung-Yi Lin, Jon Amoroso

: '''[[Molecular Playground/ACP apo]]''', Gitanjeli Prasad

Thayumanavan Lab

: '''[[Molecular Playground/Lysozime ]]''', Daniella Gonzalez

: '''[[Molecular Playground/Beta-galactosidase]]''', Judy Ventura

: '''[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]''', Krishna Reddy Raghupathi

: '''[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]''', Rami Rajasekar Reddy

: '''[[Molecular Playground/Biotin binding avidin]]''', Diego Amado

: '''[[User:Jiaming Zhuang|Molecular Playground/MMP12]]''', Jiaming Zhuang

: ''' [[User:Jing Guo|Molecular Playground/Gluconase]]''', Jing Guo

: '''[[Molecular Playground/Glutathione Reductase]]''', Reuben Chacko

Thayumanavan & Vachet Labs

: '''[[Molecular Playground/Trypsin]]''', Gladys Murage

[http://people.chem.umass.edu/thompson/index.html Thompson] & [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs

: '''[[Molecular Playground/Bacterial Chemotaxis Receptors]]''', Lynmarie K. Thompson, Shiela M. Jones

: '''[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]''', Meili Yang

[http://www.chem.umass.edu/~vachet/index.html Vachet Lab]

: '''[[Molecular playground/beta 2 microglobulin]]''', Nick Borotto
:: Best CBI Molecule Jmol scenes 2010

: '''[[Molecular Playground/Myoglobin]]''', Yuping Zhou

Other Molecules of interest

: '''[[Molecular Playground/PcrA Helicase]]''', Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]

Other Laboratories

: '''[[Molecular Playground/YKL-40]]''', Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]

: '''[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]''', Daniel Seeman, Dubin Lab

: '''[[Molecular Playground/ADAM13]]''', Genevieve Abbruzzese, Alfandari Lab

Instructions:

'''Congratulations to the prize-winning CBI molecules noted above! These also provide great examples to follow. Another prize for best CBI Molecules page and/or scene will be awarded in spring 2011!'''

Choose a molecule that is part of your research project.

1. If you don't already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.

2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description (Enter "User:your name/sandbox 1" (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]).

3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.

4. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.

5. Follow instructions at [[Molecular Playground/Procedures]] as well. But don't "capture the state script for your scene"; that will be done for you (see #7). With your chosen Jmol scene for the Molecular Playground, specify a "banner", which will be projected with the molecule on the Molecular Playground. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: "Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to "smell" their environment."

6. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter "Molecular Playground/your molecule" (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.

7. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the "Bacterial chemotaxis receptors" example above. Please list your lab group, with your name in parentheses. That way more than one name can be associated with a Molecular Playground page (if there are several students on the Molecular Playground page, please indicate your scene with your initials). It would be great to link the lab names to web pages too. Once this link is there, your scene is considered done, and someone will capture the state script for display on the Molecular Playground.

Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor

2010-12-10T21:58:18Z

Meili Yang: New page: One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at th...

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].

The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

{{Clear}}

=== Cytoplasmic domain of TSR ===

{{Clear}}
<applet load='2ho9' size='[450,338]' frame='true' align='right'
caption='Cytoplasmic domain of a serine chemotaxis receptor(1qu7)' scene='User:Meili_Yang/sandbox_1/Cytoplasmic_domain/1'>

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

User:Meili Yang/sandbox 1

2010-12-09T22:41:25Z

Meili Yang:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].

The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.''

{{Clear}}

=== Cytoplasmic domain of TSR ===

{{Clear}}
<applet load='2ho9' size='[450,338]' frame='true' align='right'
caption='Cytoplasmic domain of a serine chemotaxis receptor(1qu7)' scene='User:Meili_Yang/sandbox_1/Cytoplasmic_domain/1'>

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

User:Meili Yang/sandbox 1

2010-12-09T22:35:27Z

Meili Yang: /* Cytoplasmic domain of TSR */

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].

The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

{{Clear}}

=== Cytoplasmic domain of TSR ===

{{Clear}}
<applet load='1wat' size='[450,338]' frame='true' align='right'
caption= 'Cytoplasmic domain of a serine chemotaxis receptor(1qu7)' scene='User:Meili_Yang/sandbox_1/Cytoplasmic_domain/1'>

The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

User:Meili Yang/sandbox 1

2010-12-09T22:32:58Z

Meili Yang: /* Cytoplasmic domain */

User:Meili Yang/sandbox 1

2010-12-09T22:28:20Z

Meili Yang: /* Cytoplasmic domain */

User:Meili Yang/sandbox 1

2010-12-09T22:22:45Z

Meili Yang: /* Cytoplasmic domain */

User:Meili Yang/sandbox 1

2010-12-09T22:19:46Z

Meili Yang: /* Cytoplasmic domain */

User:Meili Yang/sandbox 1

2010-12-09T22:09:30Z

Meili Yang:

User:Meili Yang/sandbox 1

2010-12-09T22:08:31Z

Meili Yang:

[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].

The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

{{Clear}}

=== Cytoplasmic domain ===

The spinning protein (<scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'>Initial view</scene>) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).

Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to "smell" their environment.

User:Meili Yang/sandbox 1

2010-12-09T22:06:34Z

Meili Yang: New page: Bacterial chemotaxis receptor One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Ch...

[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].

The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.

Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.

{{Clear}}
<applet load='1wat' size='[450,338]' frame='true' align='right'
caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'/>

=== Cytoplasmic domain ===

The spinning protein (<scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'>Initial view</scene>) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).

Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to "smell" their environment.