Sandbox FEBS Gdansk 33 - Revision history

Student: /* Protein information */

Student — Sun, 14 Jul 2013 15:24:03 GMT

Protein information

←Older revision		Revision as of 15:24, 14 July 2013
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	== Protein information ==		== Protein information ==
	'''3du5''' is the pdb code for ''Tribolium castaneum'' telomerase catalytic subunit [[TERT]].		'''3du5''' is the pdb code for ''Tribolium castaneum'' telomerase catalytic subunit [[TERT]].
-	A common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of [[telomerase]], TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA ~~polymerases~~ and B-family DNA ~~polymerases~~. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.	+	A common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of [[telomerase]], TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral [[RNA polymerase]]s and B-family [[DNA polymerase]]s. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an [[RNA-DNA heteroduplex]] in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.

Student at 15:23, 14 July 2013

Student — Sun, 14 Jul 2013 15:23:23 GMT

←Older revision		Revision as of 15:23, 14 July 2013
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	== Protein information ==		== Protein information ==
-	'''3du5''' is the pdb code for ''Tribolium castaneum'' telomerase catalytic subunit TERT.	+	'''3du5''' is the pdb code for ''Tribolium castaneum'' telomerase catalytic subunit [[TERT]].
-	A common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of telomerase, TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.	+	A common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of [[telomerase]], TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.

Student at 15:18, 14 July 2013

Student — Sun, 14 Jul 2013 15:18:10 GMT

←Older revision		Revision as of 15:18, 14 July 2013
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-	<Structure load='3DU5' size='500' frame='true' align='right' caption=	+	<Structure load='3DU5' size='500' frame='true' align='right'
-	'~~<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>~~	+	caption='{{Template:ColorKey_ConSurf}}'
-	{{Template:ColorKey_ConSurf}}	+	scene='Insert optional scene name here' />
-	~~<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>'~~ scene='Insert optional scene name here' />	+

		+	<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>
		+
		+	<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>

	== Questions ==		== Questions ==

Student at 15:16, 14 July 2013

Student — Sun, 14 Jul 2013 15:16:04 GMT

←Older revision		Revision as of 15:16, 14 July 2013
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-	<Structure load='3DU5' size='500' frame='true' align='right' caption='	+	<Structure load='3DU5' size='500' frame='true' align='right' caption=
-	<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>	+	'<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>
	{{Template:ColorKey_ConSurf}}		{{Template:ColorKey_ConSurf}}
	<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>' scene='Insert optional scene name here' />		<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>' scene='Insert optional scene name here' />

Student at 15:15, 14 July 2013

Student — Sun, 14 Jul 2013 15:15:35 GMT

←Older revision		Revision as of 15:15, 14 July 2013
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-	<Structure load='3DU5' size='500' frame='true' align='right' caption='~~{{Template:ColorKey_ConSurf}}' scene='Insert optional scene name here' />~~	+	<Structure load='3DU5' size='500' frame='true' align='right' caption='
-		+
	<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>		<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>
	{{Template:ColorKey_ConSurf}}		{{Template:ColorKey_ConSurf}}
		+	<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>' scene='Insert optional scene name here' />

-	<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>

	== Questions ==		== Questions ==

Student at 15:14, 14 July 2013

Student — Sun, 14 Jul 2013 15:14:47 GMT

←Older revision		Revision as of 15:14, 14 July 2013
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-	<Structure load='3DU5' size='500' frame='true' align='right' caption='~~Insert caption here~~' scene='Insert optional scene name here' />	+	<Structure load='3DU5' size='500' frame='true' align='right' caption='{{Template:ColorKey_ConSurf}}' scene='Insert optional scene name here' />

	<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>		<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>

Student at 15:14, 14 July 2013

Student — Sun, 14 Jul 2013 15:14:06 GMT

←Older revision		Revision as of 15:14, 14 July 2013
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	<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>		<scene name='55/553932/3du5/1'>Conservation of 3du5</scene>
		+	{{Template:ColorKey_ConSurf}}

	<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>		<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>

Student at 15:11, 14 July 2013

Student — Sun, 14 Jul 2013 15:11:31 GMT

←Older revision		Revision as of 15:11, 14 July 2013
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	== Protein information ==		== Protein information ==
-		+	'''3du5''' is the pdb code for ''Tribolium castaneum'' telomerase catalytic subunit TERT.
-		+	A common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of telomerase, TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.
-	'''3du5''' is a common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of telomerase, TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.	+


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	<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>		<scene name='55/553932/Secondary_structure/1'>3du5 secondary structure</scene>
		+
		+	== Questions ==
		+
		+	Which residues are the most conserved through the evolution in the family of 3du5 protein?
		+	How many helixes and sheets are there?

Student at 15:04, 14 July 2013

Student — Sun, 14 Jul 2013 15:04:37 GMT

←Older revision		Revision as of 15:04, 14 July 2013
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	'''3du5''' is a common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of telomerase, TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.		'''3du5''' is a common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of telomerase, TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.

-		+
-	~~</StructureSection>~~	+
	<Structure load='3DU5' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />		<Structure load='3DU5' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Student at 15:04, 14 July 2013

Student — Sun, 14 Jul 2013 15:04:22 GMT

←Older revision		Revision as of 15:04, 14 July 2013
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	== 3du5 Structure and Evolutionary Conservation ==		== 3du5 Structure and Evolutionary Conservation ==
-	~~<StructureSection load~~=~~'1dq8' size~~=~~'350' side~~='~~right~~' ~~caption=~~'~~Structure of HMG-CoA reductase (PDB entry [[1dq8]])~~' ~~scene=~~''>	+
-	~~Anything~~ in ~~this section will appear adjacent to~~ the 3D structure and ~~will be scrollable~~.	+
		+	== Protein information ==
		+
		+
		+	'''3du5''' is a common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of telomerase, TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.
		+

	</StructureSection>		</StructureSection>