Reserved Sandbox 329 - Revision history

Jessica Lowry at 23:28, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 23:28:28 GMT

←Older revision		Revision as of 23:28, 16 March 2011
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	== STRUCTURE ==		== STRUCTURE ==

-	The uridylyl transferase bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.<ref name="primary citation">PMID:17785418</ref> Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved in TUTases, and are required for coordinating the Mg<sup>2+</sup> ions in some TUTases. <ref name="primary citation">PMID:17785418</ref> Thus, these <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are vital in ~~catalysing~~ this reaction.	+	The uridylyl transferase bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.<ref name="primary citation">PMID:17785418</ref> Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved in TUTases, and are required for coordinating the Mg<sup>2+</sup> ions in some TUTases. <ref name="primary citation">PMID:17785418</ref> Thus, these <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are vital in catalyzing this reaction.

	== REFERENCES ==		== REFERENCES ==

Jessica Lowry at 23:26, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 23:26:51 GMT

←Older revision		Revision as of 23:26, 16 March 2011
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	== '''Uridylyl transferases''' ==		== '''Uridylyl transferases''' ==

-	[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases\|Secondary structure succession of ATP-bound TUTases.]]	+	[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases. Secondary structure residues are ordered from blue to red.\|Secondary structure succession of ATP-bound TUTases.]]

	== INTRODUCTION ==		== INTRODUCTION ==

Jessica Lowry at 23:20, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 23:20:52 GMT

←Older revision		Revision as of 23:20, 16 March 2011
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	== STRUCTURE ==		== STRUCTURE ==

-	The uridylyl transferase bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.<ref name="primary citation">PMID:17785418</ref>	+	The uridylyl transferase bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.<ref name="primary citation">PMID:17785418</ref> Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved in TUTases, and are required for coordinating the Mg<sup>2+</sup> ions in some TUTases. <ref name="primary citation">PMID:17785418</ref> Thus, these <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are vital in catalysing this reaction.
-		+
-	Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved in TUTases, and are required for coordinating the Mg<sup>2+</sup> ions in some TUTases. <ref name="primary citation">PMID:17785418</ref> Thus, these <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are vital in catalysing this reaction.	+

	== REFERENCES ==		== REFERENCES ==

Jessica Lowry at 23:20, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 23:20:08 GMT

←Older revision		Revision as of 23:20, 16 March 2011
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	== INTRODUCTION ==		== INTRODUCTION ==

-	Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction ~~adding~~ UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions.<ref name="primary citation">PMID:17785418</ref>	+	Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction that adds UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions.<ref name="primary citation">PMID:17785418</ref>

	{{STRUCTURE_2q0d \| PDB=2q0d \| SCENE=Reserved_Sandbox_329/Scene1/1}}		{{STRUCTURE_2q0d \| PDB=2q0d \| SCENE=Reserved_Sandbox_329/Scene1/1}}
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	== STRUCTURE ==		== STRUCTURE ==

-	The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions.	+	The uridylyl transferase bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions, however many TUTases involved in RNA editing are shown to exhibit preference for binding to UTP instead.<ref name="primary citation">PMID:17785418</ref>
-		+
-	~~Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved~~ in ~~TUTases, and~~ are ~~required~~ for ~~coordinating the Mg<sup>2+</sup> ions in some TUTases~~. <ref name="primary citation">PMID:17785418</ref>	+

		+	Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved in TUTases, and are required for coordinating the Mg<sup>2+</sup> ions in some TUTases. <ref name="primary citation">PMID:17785418</ref> Thus, these <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are vital in catalysing this reaction.

	== REFERENCES ==		== REFERENCES ==

Jessica Lowry at 21:22, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 21:22:40 GMT

←Older revision		Revision as of 21:22, 16 March 2011
Line 5:		Line 5:
	== INTRODUCTION ==		== INTRODUCTION ==

-	Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction adding UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions~~. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group~~.<ref name="primary citation">PMID:17785418</ref>	+	Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction adding UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions.<ref name="primary citation">PMID:17785418</ref>

	{{STRUCTURE_2q0d \| PDB=2q0d \| SCENE=Reserved_Sandbox_329/Scene1/1}}		{{STRUCTURE_2q0d \| PDB=2q0d \| SCENE=Reserved_Sandbox_329/Scene1/1}}

Jessica Lowry at 21:20, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 21:20:41 GMT

←Older revision		Revision as of 21:20, 16 March 2011
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-	{{STRUCTURE_2q0d \| PDB=2q0d \| SCENE=Reserved_Sandbox_329/Scene1/1}}
-
	== '''Uridylyl transferases''' ==		== '''Uridylyl transferases''' ==

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	Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction adding UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group.<ref name="primary citation">PMID:17785418</ref>		Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction adding UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group.<ref name="primary citation">PMID:17785418</ref>
		+
		+	{{STRUCTURE_2q0d \| PDB=2q0d \| SCENE=Reserved_Sandbox_329/Scene1/1}}

	== STRUCTURE ==		== STRUCTURE ==

Jessica Lowry at 21:17, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 21:17:05 GMT

←Older revision		Revision as of 21:17, 16 March 2011
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	The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions.		The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions.

-	<scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene>	+	Three <scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene> are conserved in TUTases, and are required for coordinating the Mg<sup>2+</sup> ions in some TUTases. <ref name="primary citation">PMID:17785418</ref>
		+

	== REFERENCES ==		== REFERENCES ==

Jessica Lowry at 21:10, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 21:10:43 GMT

←Older revision		Revision as of 21:10, 16 March 2011
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	== '''Uridylyl transferases''' ==		== '''Uridylyl transferases''' ==

-		+	[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases\|Secondary structure succession of ATP-bound TUTases.]]
-	[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases\|Secondary ~~Structure Succession~~ of ATP-bound TUTases.]]	+
-		+

	== INTRODUCTION ==		== INTRODUCTION ==

-	Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group.<ref name="primary citation">PMID:17785418</ref>	+	Terminal uridylyl transferases (TUTases) belong to a superfamily of polymerase ß nucleotidyl transferases.<ref name="primary citation">PMID:17785418</ref> TUTases have been isolated from ''Trypanosoma brucei'' and also ''Leishmania'' ssp, parasites causing diseases in humans such as African Sleeping Sickness.<ref>PMID:11893335</ref> TUTases function in RNA editing; more specifically they catalyze the reaction adding UMP to a RNA substrate. Trypanosomal TUTases have RNA substrates that are shown to select for cognate nucleosides and provide a metal ion binding site for Mg<sup>2+</sup> ions. TUTases function in RNA editing; they add UMP to the 3' hydroxyl group.<ref name="primary citation">PMID:17785418</ref>

	== STRUCTURE ==		== STRUCTURE ==
Line 15:		Line 13:
	The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions.		The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions.

-		+	<scene name='Reserved_Sandbox_329/Asp/1'>aspartate residues</scene>
-		+
-	~~----~~	+
-		+
-		+
-		+

	== REFERENCES ==		== REFERENCES ==

Jessica Lowry at 19:23, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 19:23:32 GMT

←Older revision		Revision as of 19:23, 16 March 2011
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	== '''Uridylyl transferases''' ==		== '''Uridylyl transferases''' ==
		+
		+
		+	[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases\|Secondary Structure Succession of ATP-bound TUTases.]]
		+

	== INTRODUCTION ==		== INTRODUCTION ==
Line 11:		Line 15:
	The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions.		The bound [[ligand]] is an <scene name='Reserved_Sandbox_329/Ligand/4'>ATP complex</scene> with two Mg<sup>2+</sup> ions.

-	[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases\|Secondary Structure Succession of ATP-bound TUTases.]]

Jessica Lowry at 19:20, 16 March 2011

Jessica Lowry — Wed, 16 Mar 2011 19:20:38 GMT

←Older revision		Revision as of 19:20, 16 March 2011
Line 13:		Line 13:
	[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases\|Secondary Structure Succession of ATP-bound TUTases.]]		[[Image:SECONDARY_STRUCTURE_SUCCESSION.jpg\|thumb\|left\|upright=2.0\|alt=Secondary Structure Succession of ATP-bound TUTases\|Secondary Structure Succession of ATP-bound TUTases.]]

		+
		+	----