Ubiquitin Structure & Function - Revision history

Alexander Berchansky at 14:13, 18 November 2019

2019-11-18T14:13:39Z

← Older revision		Revision as of 14:13, 18 November 2019
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	Infectious agents can manipulate ubiquitin or deubiquitination and one such protein is Chlamydia trachomatis. Chlamydia trachomatis' protein Cdu-1 catalyzes the hydrolysis of ubiquitin chains from Mcl-1. When polyubiquitnated, Mcl-1 is destined to be degraded by the proteasome, lowering the level of Mcl-1 and subsequently leading to apoptosis. The activity of Cdu-1 counteracts this by removing the ubiquitin, thus leading to higher levels of Mcl-1 in the cell. Additional information can be found here [[User:Karsten Theis/5B5Q]]		Infectious agents can manipulate ubiquitin or deubiquitination and one such protein is Chlamydia trachomatis. Chlamydia trachomatis' protein Cdu-1 catalyzes the hydrolysis of ubiquitin chains from Mcl-1. When polyubiquitnated, Mcl-1 is destined to be degraded by the proteasome, lowering the level of Mcl-1 and subsequently leading to apoptosis. The activity of Cdu-1 counteracts this by removing the ubiquitin, thus leading to higher levels of Mcl-1 in the cell. Additional information can be found here [[User:Karsten Theis/5B5Q]]

			SEE ALSO [[Tumor susceptibility gene 101]]
	</StructureSection>		</StructureSection>

Joel L. Sussman at 06:26, 30 August 2018

2018-08-30T06:26:09Z

← Older revision		Revision as of 06:26, 30 August 2018
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	=Introduction=		=Introduction=
	Ubiquitin is one of the most highly conserved eukaryotic proteins. Primary structures found throughout ubiquitin are identical in all bovine, insects and human ubiquitin <ref name="mainpaper"/>. The only difference observed amongst these species is seen in the terminal Gly-Gly residues. Yeast and oat ubiquitin only differ in three of the 76 residues when compared to ubiquitin found in higher eukaryotes<ref name="mainpaper"/>.		Ubiquitin is one of the most highly conserved eukaryotic proteins. Primary structures found throughout ubiquitin are identical in all bovine, insects and human ubiquitin <ref name="mainpaper"/>. The only difference observed amongst these species is seen in the terminal Gly-Gly residues. Yeast and oat ubiquitin only differ in three of the 76 residues when compared to ubiquitin found in higher eukaryotes<ref name="mainpaper"/>.
			[[image:1ubiq.png\| thumb \|none \| upright=2.0 \|Ubiquitin structure: Arg74 in pink and Gly75 Gly76 in white.]]

	<!-- The content below was inserted by the ConSurf template -->		<!-- The content below was inserted by the ConSurf template -->
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	[http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ubq ConSurf].		[http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ubq ConSurf].
	<!-- end of content inserted by the ConSurf template -->		<!-- end of content inserted by the ConSurf template -->
	~~[[image:1ubiq.png\| thumb \|none \| upright=2.0 \|Ubiquitin structure: Arg74 in pink and Gly75 Gly76 in white.]]~~

	Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well<ref name="mainpaper"/>.		Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well<ref name="mainpaper"/>.

Joel L. Sussman at 06:25, 30 August 2018

2018-08-30T06:25:05Z

@@ Line 5: / Line 5: @@
 =Introduction=
-Ubiquitin is one of the most highly conserved eukaryotic proteins.  Primary structures found throughout ubiquitin are identical in all bovine, insects and human ubiquitin <ref name="mainpaper"/>.  The only difference observed amongst these species is seen in the terminal Gly-Gly residues.  Yeast and oat ubiquitin only differ in three of the 76 residues when compared to ubiquitin found in higher eukaryotes<ref name="mainpaper"/>.[[image:1ubiq.png| thumb |none | upright=2.0 |Ubiquitin structure: Arg74 in pink and Gly75 Gly76 in white.]]
+Ubiquitin is one of the most highly conserved eukaryotic proteins.  Primary structures found throughout ubiquitin are identical in all bovine, insects and human ubiquitin <ref name="mainpaper"/>.  The only difference observed amongst these species is seen in the terminal Gly-Gly residues.  Yeast and oat ubiquitin only differ in three of the 76 residues when compared to ubiquitin found in higher eukaryotes<ref name="mainpaper"/>.
 Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well<ref name="mainpaper"/>.

Joel L. Sussman at 06:22, 30 August 2018

2018-08-30T06:22:57Z

← Older revision		Revision as of 06:22, 30 August 2018
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	<StructureSection load='1ubq' size='350' side='right' caption='Human ubiquitin, [[1ubq]])' scene=''>		<StructureSection load='1ubq' size='350' side='right' caption='Human ubiquitin, [[1ubq]])' scene=''>

	[[Ubiquitin]] is a single 8565 M<sub>r</sub> polypeptide consisting of 76 amino acid residues~~. Ubiquitin~~ is highly known for its role in ATP-dependent protein degradation<ref name="mainpaper">PMID: 3041007</ref>		[[Ubiquitin]] is a single 8565 M<sub>r</sub> polypeptide consisting of 76 amino acid residues and is highly known for its role in ATP-dependent protein degradation<ref name="mainpaper">PMID: 3041007</ref>

Joel L. Sussman at 06:22, 30 August 2018

2018-08-30T06:22:18Z

← Older revision		Revision as of 06:22, 30 August 2018
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	~~==Ubiquitin Structure & Function==~~
	<StructureSection load='1ubq' size='350' side='right' caption='Human ubiquitin, [[1ubq]])' scene=''>		<StructureSection load='1ubq' size='350' side='right' caption='Human ubiquitin, [[1ubq]])' scene=''>

Joel L. Sussman at 06:21, 30 August 2018

2018-08-30T06:21:46Z

← Older revision		Revision as of 06:21, 30 August 2018
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	==~~Your Heading Here (maybe something like '~~Structure')==		==Ubiquitin Structure & Function==
	<StructureSection load='1ubq' size='350' side='right' caption='Human ubiquitin, [[1ubq]])' scene=''>		<StructureSection load='1ubq' size='350' side='right' caption='Human ubiquitin, [[1ubq]])' scene=''>

Joel L. Sussman at 06:20, 30 August 2018

2018-08-30T06:20:53Z

← Older revision		Revision as of 06:20, 30 August 2018
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	==Your Heading Here (maybe something like 'Structure')==		==Your Heading Here (maybe something like 'Structure')==
	<StructureSection load='~~3rec~~' size='350' side='right' caption='~~Escherichia coli reca protein-bound DNA (PDB entry~~ [[~~3rec~~]])' scene=''>		<StructureSection load='1ubq' size='350' side='right' caption='Human ubiquitin, [[1ubq]])' scene=''>

	~~Anything in this section will appear adjacent to the 3D structure and will be scrollable.~~



	[[Ubiquitin]] is a single 8565 M<sub>r</sub> polypeptide consisting of 76 amino acid residues. Ubiquitin is highly known for its role in ATP-dependent protein degradation<ref name="mainpaper">PMID: 3041007</ref>		[[Ubiquitin]] is a single 8565 M<sub>r</sub> polypeptide consisting of 76 amino acid residues. Ubiquitin is highly known for its role in ATP-dependent protein degradation<ref name="mainpaper">PMID: 3041007</ref>
	~~{{STRUCTURE_1ubq\| PDB=1ubq \| SIZE=400\| SCENE= \|right\|CAPTION=Human ubiquitin, [[1ubq]] }}~~

Joel L. Sussman at 06:18, 30 August 2018

2018-08-30T06:18:25Z

← Older revision		Revision as of 06:18, 30 August 2018
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			==Your Heading Here (maybe something like 'Structure')==
			<StructureSection load='3rec' size='350' side='right' caption='Escherichia coli reca protein-bound DNA (PDB entry [[3rec]])' scene=''>

			Anything in this section will appear adjacent to the 3D structure and will be scrollable.



	[[Ubiquitin]] is a single 8565 M<sub>r</sub> polypeptide consisting of 76 amino acid residues. Ubiquitin is highly known for its role in ATP-dependent protein degradation<ref name="mainpaper">PMID: 3041007</ref>		[[Ubiquitin]] is a single 8565 M<sub>r</sub> polypeptide consisting of 76 amino acid residues. Ubiquitin is highly known for its role in ATP-dependent protein degradation<ref name="mainpaper">PMID: 3041007</ref>
	{{STRUCTURE_1ubq\| PDB=1ubq \| SIZE=400\| SCENE= \|right\|CAPTION=Human ubiquitin, [[1ubq]] }}		{{STRUCTURE_1ubq\| PDB=1ubq \| SIZE=400\| SCENE= \|right\|CAPTION=Human ubiquitin, [[1ubq]] }}
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	Infectious agents can manipulate ubiquitin or deubiquitination and one such protein is Chlamydia trachomatis. Chlamydia trachomatis' protein Cdu-1 catalyzes the hydrolysis of ubiquitin chains from Mcl-1. When polyubiquitnated, Mcl-1 is destined to be degraded by the proteasome, lowering the level of Mcl-1 and subsequently leading to apoptosis. The activity of Cdu-1 counteracts this by removing the ubiquitin, thus leading to higher levels of Mcl-1 in the cell. Additional information can be found here [[User:Karsten Theis/5B5Q]]		Infectious agents can manipulate ubiquitin or deubiquitination and one such protein is Chlamydia trachomatis. Chlamydia trachomatis' protein Cdu-1 catalyzes the hydrolysis of ubiquitin chains from Mcl-1. When polyubiquitnated, Mcl-1 is destined to be degraded by the proteasome, lowering the level of Mcl-1 and subsequently leading to apoptosis. The activity of Cdu-1 counteracts this by removing the ubiquitin, thus leading to higher levels of Mcl-1 in the cell. Additional information can be found here [[User:Karsten Theis/5B5Q]]
			</StructureSection>

	==3D structures of ubiqitin==		==3D structures of ubiqitin==

Karsten Theis: /* Diseases */

2018-04-30T17:46:16Z

Diseases

← Older revision		Revision as of 17:46, 30 April 2018
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	There are numerous diseases that may develop as a result of ubiquitin abnormalities. There are two disease categories possible in non-lethal states. One being the result of function loss and the other being function gain. Loss of function may occur due to a target substrate mutation or a mutation in a ubiquitin enzyme causing protein stabilization and a decrease in protein degradation. Function gain, on the other hand, results in an increase in protein degradation.		There are numerous diseases that may develop as a result of ubiquitin abnormalities. There are two disease categories possible in non-lethal states. One being the result of function loss and the other being function gain. Loss of function may occur due to a target substrate mutation or a mutation in a ubiquitin enzyme causing protein stabilization and a decrease in protein degradation. Function gain, on the other hand, results in an increase in protein degradation.
	Cancer may result from either case. Oncoproteins may become stabilized while tumor suppressor genes may become destabilized. Liddle's Syndrome is a type of early-onset hypertension<ref name="liddles">PMID: 8521520</ref>. Sodium ions and water are excessively reabsorbed caused by E3 ligase non-recognition. Angleman syndrome is caused by a E3 ligase defect. This defect causes affects in human brain development resulting in symptoms such as mental retardation, seizures and abnormal gait. Lastly, neurogenetive diseases are caused by the accumulation of ubiquitin-conjugates. Diseases of this nature include Alzheimers and Parkinson's.		Cancer may result from either case. Oncoproteins may become stabilized while tumor suppressor genes may become destabilized. Liddle's Syndrome is a type of early-onset hypertension<ref name="liddles">PMID: 8521520</ref>. Sodium ions and water are excessively reabsorbed caused by E3 ligase non-recognition. Angleman syndrome is caused by a E3 ligase defect. This defect causes affects in human brain development resulting in symptoms such as mental retardation, seizures and abnormal gait. Lastly, neurogenetive diseases are caused by the accumulation of ubiquitin-conjugates. Diseases of this nature include Alzheimers and Parkinson's.

			Infectious agents can manipulate ubiquitin or deubiquitination and one such protein is Chlamydia trachomatis. Chlamydia trachomatis' protein Cdu-1 catalyzes the hydrolysis of ubiquitin chains from Mcl-1. When polyubiquitnated, Mcl-1 is destined to be degraded by the proteasome, lowering the level of Mcl-1 and subsequently leading to apoptosis. The activity of Cdu-1 counteracts this by removing the ubiquitin, thus leading to higher levels of Mcl-1 in the cell. Additional information can be found here [[User:Karsten Theis/5B5Q]]

	==3D structures of ubiqitin==		==3D structures of ubiqitin==

	[[Ubiquitin]]		[[Ubiquitin]]

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

Michal Harel at 08:50, 20 September 2011

2011-09-20T08:50:21Z

← Older revision		Revision as of 08:50, 20 September 2011
Line 36:		Line 36:
	There are numerous diseases that may develop as a result of ubiquitin abnormalities. There are two disease categories possible in non-lethal states. One being the result of function loss and the other being function gain. Loss of function may occur due to a target substrate mutation or a mutation in a ubiquitin enzyme causing protein stabilization and a decrease in protein degradation. Function gain, on the other hand, results in an increase in protein degradation.		There are numerous diseases that may develop as a result of ubiquitin abnormalities. There are two disease categories possible in non-lethal states. One being the result of function loss and the other being function gain. Loss of function may occur due to a target substrate mutation or a mutation in a ubiquitin enzyme causing protein stabilization and a decrease in protein degradation. Function gain, on the other hand, results in an increase in protein degradation.
	Cancer may result from either case. Oncoproteins may become stabilized while tumor suppressor genes may become destabilized. Liddle's Syndrome is a type of early-onset hypertension<ref name="liddles">PMID: 8521520</ref>. Sodium ions and water are excessively reabsorbed caused by E3 ligase non-recognition. Angleman syndrome is caused by a E3 ligase defect. This defect causes affects in human brain development resulting in symptoms such as mental retardation, seizures and abnormal gait. Lastly, neurogenetive diseases are caused by the accumulation of ubiquitin-conjugates. Diseases of this nature include Alzheimers and Parkinson's.		Cancer may result from either case. Oncoproteins may become stabilized while tumor suppressor genes may become destabilized. Liddle's Syndrome is a type of early-onset hypertension<ref name="liddles">PMID: 8521520</ref>. Sodium ions and water are excessively reabsorbed caused by E3 ligase non-recognition. Angleman syndrome is caused by a E3 ligase defect. This defect causes affects in human brain development resulting in symptoms such as mental retardation, seizures and abnormal gait. Lastly, neurogenetive diseases are caused by the accumulation of ubiquitin-conjugates. Diseases of this nature include Alzheimers and Parkinson's.

			==3D structures of ubiqitin==

			[[Ubiquitin]]
	=References=		=References=
	<references/>		<references/>