Proteopedia - User contributions [en]

Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

2015-01-25T09:39:36Z

Raya Liberman:

<StructureSection load='2c1z' size='340' side='right' caption='Caption for this structure' scene=''>
Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT) is involved in the modification of grape anthocyanins (a plant pigment) and thus could affect their water solubility and color stability. The addition of a sugar molecule on the anthocyanin is a preliminary step to its transport to the cell vacuole. The transfer to the vacuole is important for the pigment accumulation. The anthocyanin accumulation plays a significant role in quality of agricultural produce, as it affects fruit color and its health benefits as a natural antioxidant. This enzyme affects the quality of both table grapes and wine grapes.
== Introduction ==

Vv3GT belongs to Glycosyltransferases (GTs), a large family of enzymes involved in the transfer of sugar residues from a sugar donor to various substrates. Glycosylation of metabolites in plants is usually catalyzed by glycosyltransferases (GTs) belonging to the GT1 sub-family (as classified by the CAZy database [http://www.cazy.org], which use UDP-activated sugars as the major donor molecule and are thus referred to as UGTs. The Glycosyltransferase activity is highly important for the synthesis of thousands of plant metabolites. This enzymes differ in their specificity for substrate, position of glycosylation on the substrate and recognition of sugar donor. These differences are important and could affect the function and stability of the metabolite. A good example for the importance of glycosyltransferase specificity is shown in Citrus. the difference in the position of glycosylation affects fruit flavor. Glycosylation of one position lids to the synthesis of bitter substances while the addition of same molecule at a different position lids to the synthesis of tasteless substances.

== Relevance ==

== Structural highlights ==

Despite low primary sequence similarity, the secondary and tertiary structures of GTs are highly conserved. <ref>PMID:16482224</ref>

=== GT-B ===

Plant glycosyltransferases assume one of two folds, GT-A or GT-B. Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
The <scene name='69/692252/2c1z_rainbow/1'>N-terminal and C-terminal domain</scene>, linked by a flexible loop and α-helix with a hinge region. The linker could be important for sugar donor binding. This linker region holds the UDP-sugar donor next to the C-terminal PSPG motif. The C-terminal domain is highly conserved and binds the UDP sugar donor (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.

{{Template:ColorKey_N52C3Rainbow}}

[[Image:2C1Z GT-B b.png|frame|alt=Puzzle globe| Vv3GT with the two Rossmann-like domains]]

=== PSPG ===

The plant UGTs are characterized by sharing a highly conserved 44 amino acid motif referred to as the
<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif). Amino acids of the PSPG motif provide most of the interactions with the sugar donor molecule. 10 highly conserved residues of the 44 amino acid PSPG motif are observed to directly interact with the UDP-sugar. In Vv3GT the PSPG motif begins with Pro 334 and ends with Gln 375.

Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.

== Quiz ==

</StructureSection>

== References ==
1. Frydman A, Weisshaus O, Bar-Peled M, Huhman DV, Sumner LW, Marin FR, Lewinsohn E, Fluhr R, Gressel J and Eyal Y (2004) Citrus fruit bitter flavors: Isolation and functional characterization of the gene Cm1,2RhaT encoding a 1,2 rhamnosyltransferase, a key enzyme in the biosynthesis of the bitter flavonoids of citrus. Plant J. 40: 88-100.

2. Offen W, Martinez-Fleites C, Yang M, Lim EK, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ (2006) Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO 25: 1396-1405.

3. Osmani SA, Bak S, Møller BL (2009) Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling. Phytochemistry 70: 325-347.

Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

2015-01-25T08:58:00Z

Raya Liberman:

<StructureSection load='2c1z' size='340' side='right' caption='Caption for this structure' scene=''>
Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT) is involved in the modification of grape anthocyanins (a plant pigment) and thus could affect their water solubility and color stability. the addition of a sugar molecule on the anthocyanin is a preliminary step to its transport to the cell vacuole. The transfer to the vacuole is important for the pigment accumulation. The anthocyanin accumulation plays a significant role in quality of agricultural produce, as it affects fruit color and its health benefits as a natural antioxidant. This enzyme affects the quality of both table grapes and wine grapes.
== Introduction ==

Vv3GT belongs to Glycosyltransferases (GTs), a large family of enzymes involved in the transfer of sugar residues from a sugar donor to various substrates. Glycosylation of metabolites in plants is usually catalyzed by glycosyltransferases (GTs) belonging to the GT1 sub-family (as classified by the CAZy database [http://www.cazy.org], which use UDP-activated sugars as the major donor molecule and are thus referred to as UGTs.

== Relevance ==

== Structural highlights ==

Despite low primary sequence similarity, the secondary and tertiary structures of GTs are highly conserved. <ref>PMID:16482224</ref>

=== GT-B ===

Plant glycosyltransferases assume one of two folds, GT-A or GT-B. Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
The <scene name='69/692252/2c1z_rainbow/1'>N-terminal and C-terminal domain</scene>, linked by a flexible loop and α-helix with a hinge region. The linker could be important for sugar donor binding. This linker region holds the UDP-sugar donor next to the C-terminal PSPG motif. The C-terminal domain is highly conserved and binds the UDP sugar donor (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.

{{Template:ColorKey_N52C3Rainbow}}

[[Image:2C1Z GT-B b.png|frame|alt=Puzzle globe| Vv3GT with the two Rossmann-like domains]]

=== PSPG ===

The plant UGTs are characterized by sharing a highly conserved 44 amino acid motif referred to as the
<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif). Amino acids of the PSPG motif provide most of the interactions with the sugar donor molecule. 10 highly conserved residues of the 44 amino acid PSPG motif are observed to directly interact with the UDP-sugar. In Vv3GT the PSPG motif begins with Pro 334 and ends with Gln 375.

Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.

== Quiz ==

</StructureSection>

== References ==
1. Offen W, Martinez-Fleites C, Yang M, Lim EK, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ (2006) Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO 25: 1396-1405.

2. Osmani SA, Bak S, Møller BL (2009) Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling. Phytochemistry 70: 325-347.

Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

2015-01-25T08:36:32Z

Raya Liberman:

<StructureSection load='2c1z' size='340' side='right' caption='Caption for this structure' scene=''>
Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT) is involved in the modification of grape anthocyanins and thus could affect their color stability. The color plays a significant role in the in agricultural produce, such as table grapes and wine.
== Introduction ==

Vv3GT belongs to Glycosyltransferases (GTs), a large family of enzymes involved in the transfer of sugar residues from a sugar donor to various substrates. Glycosylation of metabolites in plants is usually catalyzed by glycosyltransferases (GTs) belonging to the GT1 sub-family (as classified by the CAZy database [http://www.cazy.org], which use UDP-activated sugars as the major donor molecule and are thus referred to as UGTs.

== Relevance ==

== Structural highlights ==

Despite low primary sequence similarity, the secondary and tertiary structures of GTs are highly conserved. <ref>PMID:16482224</ref>

=== GT-B ===

Plant glycosyltransferases assume one of two folds, GT-A or GT-B. Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
The <scene name='69/692252/2c1z_rainbow/1'>N-terminal and C-terminal domain</scene>, linked by a flexible loop and α-helix with a hinge region. The linker could be important for sugar donor binding. This linker region holds the UDP-sugar donor next to the C-terminal PSPG motif. The C-terminal domain is highly conserved and binds the UDP sugar donor (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.

{{Template:ColorKey_N52C3Rainbow}}

[[Image:2C1Z GT-B b.png|frame|alt=Puzzle globe| Vv3GT with the two Rossmann-like domains]]

=== PSPG ===

The plant UGTs are characterized by sharing a highly conserved 44 amino acid motif referred to as the
<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif). Amino acids of the PSPG motif provide most of the interactions with the sugar donor molecule. 10 highly conserved residues of the 44 amino acid PSPG motif are observed to directly interact with the UDP-sugar. In Vv3GT the PSPG motif begins with Pro 334 and ends with Gln 375.

Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.

== Quiz ==

</StructureSection>

== References ==
1. Offen W, Martinez-Fleites C, Yang M, Lim EK, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ (2006) Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO 25: 1396-1405.

2. Osmani SA, Bak S, Møller BL (2009) Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling. Phytochemistry 70: 325-347.

Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

2015-01-25T08:24:51Z

Raya Liberman:

<StructureSection load='2c1z' size='340' side='right' caption='Caption for this structure' scene=''>
Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT) is involved in the modification of grape anthocyanins and thus could affect their color stability. The color plays a significant role in the in agricultural produce, such as table grapes and wine.
== Introduction ==

Vv3GT belongs to Glycosyltransferases (GTs), a large family of enzymes involved in the transfer of sugar residues from a sugar donor to various substrates. Glycosylation of metabolites in plants is usually catalyzed by glycosyltransferases (GTs) belonging to the GT1 sub-family (as classified by the CAZy database [http://www.cazy.org], which use UDP-activated sugars as the major donor molecule and are thus referred to as UGTs.

== Relevance ==

== Structural highlights ==

Despite low primary sequence similarity, the secondary and tertiary structures of GTs are highly conserved. <ref>PMID:16482224</ref>

=== GT-B ===

Plant glycosyltransferases assume one of two folds, GT-A or GT-B. Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
The <scene name='69/692252/2c1z_rainbow/1'>N-terminal and C-terminal domain</scene>, linked by a flexible loop and α-helix with a hinge region. The linker could be important for sugar donor binding. This linker region holds the UDP-sugar donor next to the C-terminal PSPG motif. The C-terminal domain is highly conserved and binds the UDP sugar donor (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.

{{Template:ColorKey_N52C3Rainbow}}

[[Image:2C1Z GT-B b.png|frame|alt=Puzzle globe| Vv3GT with the two Rossmann-like domains]]

=== PSPG ===

The plant UGTs are characterized by sharing a highly conserved 44 amino acid motif referred to as the
<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif). Amino acids of the PSPG motif provide most of the interactions with the sugar donor molecule.

Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.

== Quiz ==

</StructureSection>

== References ==
1. Offen W, Martinez-Fleites C, Yang M, Lim EK, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ (2006) Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO 25: 1396-1405.

2. Osmani SA, Bak S, Møller BL (2009) Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling. Phytochemistry 70: 325-347.

Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

2015-01-25T08:21:31Z

Raya Liberman:

<StructureSection load='2c1z' size='340' side='right' caption='Caption for this structure' scene=''>
Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT) is involved in the modification of grape anthocyanins and thus could affect their color stability. The color plays a significant role in the in agricultural produce, such as table grapes and wine.
== Introduction ==

Vv3GT belongs to Glycosyltransferases (GTs), a large family of enzymes involved in the transfer of sugar residues from a sugar donor to various substrates. Glycosylation of metabolites in plants is usually catalyzed by glycosyltransferases (GTs) belonging to the GT1 sub-family (as classified by the CAZy database [http://www.cazy.org], which use UDP-activated sugars as the major donor molecule and are thus referred to as UGTs.

== Relevance ==

== Structural highlights ==

Despite low primary sequence similarity, the secondary and tertiary structures of GTs are highly conserved. <ref>PMID:16482224</ref>

=== GT-B ===

Plant glycosyltransferases assume one of two folds, GT-A or GT-B. Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
The <scene name='69/692252/2c1z_rainbow/1'>N-terminal and C-terminal domain</scene>, linked by a flexible loop and α-helix with a hinge region. The linker could be important for sugar donor binding. This linker region holds the UDP-sugar donor next to the C-terminal PSPG motif. The C-terminal domain is highly conserved and binds the UDP sugar donor (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.

{{Template:ColorKey_N52C3Rainbow}}

[[Image:2C1Z GT-B b.png|frame|alt=Puzzle globe| Vv3GT with the two Rossmann-like domains]]

=== PSPG ===

The plant UGTs are characterized by sharing a highly conserved 44 amino acid motif referred to as the
<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif). Amino acids of the PSPG motif provide most of the interactions with the sugar donor molecule.

Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.

== Quiz ==

</StructureSection>

== References ==
<references/>

Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

2015-01-25T08:12:37Z

Raya Liberman:

<StructureSection load='2c1z' size='340' side='right' caption='Caption for this structure' scene=''>
Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT) is involved in the modification of grape anthocyanins and thus could affect their color stability. The color plays a significant role in the in agricultural produce, such as table grapes and wine.
== Introduction ==

Vv3GT belongs to Glycosyltransferases (GTs), a large family of enzymes involved in the transfer of sugar residues from a sugar donor to various substrates. Glycosylation of metabolites in plants is usually catalyzed by glycosyltransferases (GTs) belonging to the GT1 sub-family (as classified by the CAZy database [http://www.cazy.org], which use UDP-activated sugars as the major donor molecule and are thus referred to as UGTs.

== Relevance ==

== Structural highlights ==

Despite low primary sequence similarity, the secondary and tertiary structures of GTs are highly conserved. <ref>PMID:16482224</ref>

=== GT-B ===

Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
The <scene name='69/692252/2c1z_rainbow/1'>N-terminal and C-terminal domain</scene>, linked by a flexible loop and α-helix with a hinge region. The C-terminal domain is highly conserved and binds the cosubstrate (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.

{{Template:ColorKey_N52C3Rainbow}}

[[Image:2C1Z GT-B b.png|frame|alt=Puzzle globe| Vv3GT with the two Rossmann-like domains]]

=== PSPG ===

The plant UGTs are characterized by sharing a highly conserved motif referred to as the
<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif).

Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.

== Quiz ==

</StructureSection>

== References ==
<references/>

Sandbox YOURSCHOOL 33

2014-11-23T14:19:42Z

Raya Liberman:

== 'Sandbox YOURSCHOOL 33 Structure'==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
'''Sandbox YOURSCHOOL 33'''

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow

<quiz display=simple>
{How many alpha helices are in this structure?
|type="[]"}
- None.
+ One.
- Four.
</quiz>

== 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 YOURSCHOOL 33

2014-11-23T14:19:18Z

Raya Liberman:

== 'Sandbox YOURSCHOOL 33 Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
'''Sandbox YOURSCHOOL 33'''.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow

<quiz display=simple>
{How many alpha helices are in this structure?
|type="[]"}
- None.
+ One.
- Four.
</quiz>

== 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 YOURSCHOOL 33

2014-11-23T14:18:36Z

Raya Liberman:

== 'Sandbox YOURSCHOOL 33 Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow

<quiz display=simple>
{How many alpha helices are in this structure?
|type="[]"}
- None.
+ One.
- Four.
</quiz>

== 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 YOURSCHOOL 33

2014-11-23T14:18:06Z

Raya Liberman:

==Your Heading Here (maybe something like 'Sandbox YOURSCHOOL 33 Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow

<quiz display=simple>
{How many alpha helices are in this structure?
|type="[]"}
- None.
+ One.
- Four.
</quiz>

== 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 YOURSCHOOL 33

2014-11-23T14:12:53Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow

<quiz display=simple>
{How many alpha helices are in this structure?
|type="[]"}
- None.
+ One.
- Four.
</quiz>

== 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 YOURSCHOOL 33

2014-11-23T14:10:52Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow

== 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 YOURSCHOOL 33

2014-11-23T14:10:24Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene>in this protein. Alpha helix appears in red, beta sheet in yellow

== 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 YOURSCHOOL 33

2014-11-23T14:09:51Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Let us color the two main forms of regular Secondary Structure <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene>in this protein. Alpha helix appears in red, beta sheet in yellow

== 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 YOURSCHOOL 33

2014-11-23T14:07:39Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

Secondary Structure <scene name='60/609846/Secondary_structure/1'>Secondary Structure</scene>

== 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 YOURSCHOOL 33

2014-11-23T14:06:29Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

<Secondary Structure='60/609846/Secondary_structure/1'>Secondary Structure</scene>

== 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 YOURSCHOOL 33

2014-11-23T13:56:22Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>'N to C sequence'</scene>

{{Template:ColorKey_523Rainbow}}

== 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 YOURSCHOOL 33

2014-11-23T13:55:26Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>Click here</scene>

'N to C sequence' {{Template:ColorKey_523Rainbow}}

== 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 YOURSCHOOL 33

2014-11-23T13:53:06Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>Click here</scene>

{{Template:ColorKey_523Rainbow}}

== 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 YOURSCHOOL 33

2014-11-23T13:49:41Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

N_to_c_rainbow <scene name='60/609846/N_to_c_rainbow/1'>Click here</scene>

== 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 YOURSCHOOL 33

2014-11-23T13:48:06Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='1pgb''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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.

<scene name='60/609846/N_to_c_rainbow/1'>TextToBeDisplayed</scene>

== 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 YOURSCHOOL 33

2014-11-23T13:36:17Z

Raya Liberman:

Sandbox YOURSCHOOL 33

2014-11-23T13:31:59Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load= '1pgb' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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 YOURSCHOOL 33

2014-11-23T13:28:34Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1acj' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.

[[Image:MW_Folding_Simulations.gif]]

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 YOURSCHOOL 33

2014-11-23T13:22:46Z

Raya Liberman:

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1acj' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. 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 YOURSCHOOL 33

2014-11-23T13:13:06Z

Raya Liberman: New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox YOURSCHOOL 33'''. 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/>