Proteopedia - User contributions [en]

Sandbox Reserved 1578

2019-12-01T20:18:11Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswitch==

==Overview==

<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SAM) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name="ref1">PMID:16810258</ref>

== Structural Highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand, as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions. <ref name="ref1" />

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (purple). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix. <ref name="ref1" />

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(orange). <ref name="ref1" />

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch, the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed previously hold the ligand in place for productive binding, and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. <ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

Sandbox Reserved 1578

2019-11-30T18:15:22Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswitch==

==Overview==

<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SAM) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name="ref1">PMID:16810258</ref>

== Structural Highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions. <ref name="ref1" />

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (purple). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix. <ref name="ref1" />

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(orange). <ref name="ref1" />

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. <ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

Sandbox Reserved 1578

2019-11-30T18:12:18Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswitch==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SAM) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name="ref1">PMID:16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions. <ref name="ref1" />

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (purple). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix. <ref name="ref1" />

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(orange). <ref name="ref1" />

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. <ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

Sandbox Reserved 1578

2019-11-30T18:11:14Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswitch==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name="ref1">PMID:16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions. <ref name="ref1" />

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (purple). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix. <ref name="ref1" />

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(orange). <ref name="ref1" />

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. <ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

Sandbox Reserved 1578

2019-11-30T17:10:21Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswitch==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name=“ref1">PMID:16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions. <ref name="ref1" />

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (purple). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.<ref name="ref1" />

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(orange). <ref name="ref1" />

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression.<ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.
(2) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

Sandbox Reserved 1578

2019-11-30T17:08:53Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswith==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name=“ref1">PMID:16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions. <ref name="ref1" />

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (purple). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.<ref name="ref1" />

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(orange). <ref name="ref1" />

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression.<ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.
(2) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

Sandbox Reserved 1578

2019-11-30T17:06:55Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name=“ref1">PMID:16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions. <ref name="ref1" />

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (purple). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.<ref name="ref1" />

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(orange). <ref name="ref1" />

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression.<ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

<referneces/>

Sandbox Reserved 1578

2019-11-30T16:56:00Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name=“ref1">PMID:16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (in color). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(color).

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression.

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

<referneces/>

Sandbox Reserved 1578

2019-11-30T16:54:25Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name=“ref1">PMID:16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (in color). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(color).

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression.<ref name="ref1" />

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

<referneces/>

Sandbox Reserved 1578

2019-11-30T00:30:37Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref name=“Riboswitch"> PMID: 16810258 </ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (in color). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(color).

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression.

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

<referneces/>

Sandbox Reserved 1578

2019-11-30T00:25:03Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref>PMID 16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (in color). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(color).

== Function ==

Most responses to stimuli are mediated by transcription factors that in some way either turn on or off the production of their regulatory target. Genetic regulation by RNA is often used in bacterial cells. In the use of the SAM riboswitch the aptamer of tertiary RNA will bind to the SAM ligand where the helices and nucleotides discussed before hold the ligand in place for productive binding and also folds around the tertiary RNA once binding takes place. Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression.

== References ==
(1) Montange, R. K.; Batey, R. T. Structure of the S-Adenosylmethionine Riboswitch Regulatory MRNA Element. Nature 2006, 441 (7097), 1172–1175. https://doi.org/10.1038/nature04819.

<referneces/>

Sandbox Reserved 1578

2019-11-29T18:45:19Z

Sarah Moffett:

<scene name='82/824623/Helix_interactions/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<Structure load='2gis' size='350' frame='true' align='right' caption='SAM Riboswitch' scene='SAM Riboswitch' />
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.<ref>PMID 16810258</ref>

== Structural highlights ==

The key architecture of SAM riboswitch is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The SAM ligand is bound within a pocket created by the <scene name='82/824623/Helix_interaction/2'>Helix Interaction</scene> (in color). The SAM ligand adopts a compact conformation in which the methionine stacks upon the adenine ring, stabilized in part by the π-cation interaction with the amino group pointing toward the adenine ring. Also the compact configuration of SAM creates a hydrogen bonding interaction to helix P3 and van der Waals forces interacting with the minor groove of the P1 helix.

The adenine ring of SAM is the central position between five nucleotides. The nucleotides interact by hydrogen bond attractions between themselves and the SAM ligand to stabilize position <scene name='82/824623/Nitrogenous_base_interactions/3'>Nucleotide Interaction</scene>(color).

== Function ==

Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The adenine base of SAM, A45 and U57, creates a hydrogen bonding interaction to

== References ==
<references/>

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2019-11-29T17:04:05Z

Sarah Moffett:

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2019-11-29T16:56:40Z

Sarah Moffett:

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2019-11-29T16:39:59Z

Sarah Moffett:

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2019-11-29T14:54:14Z

Sarah Moffett:

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2019-11-29T13:58:33Z

Sarah Moffett:

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2019-11-29T03:37:54Z

Sarah Moffett:

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2019-11-29T02:09:05Z

Sarah Moffett:

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2019-11-29T00:14:06Z

Sarah Moffett:

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2019-11-29T00:04:49Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.

== Function ==

Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The adenine base of SAM, A45 and U57, creates a hydrogen bonding interaction to

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">helix interaction</scene> by Group, and another to make <scene name="/12/3456/Sample/2">nitrogenous base interaction</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-20T17:45:29Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.

== Function ==

Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

The adenine base of SAM, A45 and U57, creates a hydrogen bonding interaction to

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-20T17:07:48Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.

== Function ==

Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-20T00:11:29Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch, which are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.

== Function ==

Stable binding of SAM when adequate amounts are present results in it acting as a transcriptional terminator which turns off gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-20T00:10:05Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch, which are are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.

== Function ==

Stable binding of SAM when adequate amounts are present acts as a transcriptional terminator which turns off gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-19T23:54:47Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch, which are are structured noncoding RNA domains that selectively bind metabolites and control gene expression. Nearly all examples of the known riboswitches reside in noncoding regions of messenger RNAs where they control transcription or translation.

== Function ==

In the presence of sufficient SAM riboswitch (S-adenosylmethionine), the riboswitch will bind to mRNA preventing transcription and therefore, halting gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-19T23:43:40Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch with the ability for gene regulation. The genetic regulation is driven by the binding of SAM to mRNA often in the location of the 5'-untranslated regions of mRNA in bacteria. Stable binding of SAM to mRNA causes transcriptional termination, which results in the gene at the site of binding not being expressed.

== Function ==

In the presence of sufficient SAM riboswitch (S-adenosylmethionine), the riboswitch will bind to mRNA preventing transcription and therefore, halting gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-19T23:38:12Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
S-adenosylmethionine (SMA) is a riboswitch with the ability for gene regulation. The genetic regulation is driven by the binding of SAM to mRNA often in the location of the 5'-untranslated regions of mRNA in bacteria.

== Function ==

In the presence of sufficient SAM riboswitch (S-adenosylmethionine), the riboswitch will bind to mRNA preventing transcription and therefore, halting gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-18T16:01:07Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

In the presence of sufficient SAM riboswitch (S-adenosylmethionine), the riboswitch will bind to mRNA preventing transcription and therefore, halting gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-18T14:46:51Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
In the presence of sufficient SAM riboswitch (S-adenosylmethionine), the riboswitch will bind to mRNA preventing transcription and therefore, halting gene expression. To understand the function and specificity of SAM as a riboregulator it is important to first understand the key structures of SAM. The key architecture of SAM is composed of ligand-induced interactions between one helix and the 3' side of another helix surrounding the SAM ligand as well as hydrogen bonding interactions between the adenosine base of SAM and interactions between the main chain atoms of methionine with nucleotide interactions.

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-11-18T13:58:31Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==SAM Riboswith (2GIS)==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1578

2019-10-30T15:55:20Z

Sarah Moffett:

{{Sandbox_Reserved_JMeans}}
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load=2gis' size='340' side='right' caption='SAM riboswitch' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>