Chaperone protein ClpB - Revision history

Michal Harel at 10:31, 2 June 2024

Michal Harel — Sun, 02 Jun 2024 10:31:07 GMT

←Older revision		Revision as of 10:31, 2 June 2024
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	== Disease ==		== Disease ==

-	~~CLPb~~ deficiency is a rare disorder characterized by neurological problems and shortage of white blood cells<ref>PMID:27891836</ref>. ClpB mutations cause progressive brain atrophy<ref>PMID:25597510</ref>.	+	ClpB deficiency is a rare disorder characterized by neurological problems and shortage of white blood cells<ref>PMID:27891836</ref>. ClpB mutations cause progressive brain atrophy<ref>PMID:25597510</ref>.

	== Structural highlights ==		== Structural highlights ==

Alexander Berchansky at 13:00, 7 July 2022

Alexander Berchansky — Thu, 07 Jul 2022 13:00:49 GMT

←Older revision		Revision as of 13:00, 7 July 2022
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	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, first nucleotide-binding domain <scene name='91/916397/Cv/4'>(NBD1)</scene>, a long coiled-coil <scene name='91/916397/Cv/5'>linker</scene> domain, a <scene name='91/916397/Cv/6'>second NBD</scene> and a <scene name='91/916397/Cv/7'>D2 small domain</scene>. The <scene name='91/916397/Cv/8'>first nucleotide AMPPNP binding site</scene> at NBD1 includes several hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.	+	The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, first nucleotide-binding domain <scene name='91/916397/Cv/4'>(NBD1)</scene>, a long coiled-coil <scene name='91/916397/Cv/5'>linker</scene> domain, a <scene name='91/916397/Cv/6'>second NBD</scene> and a <scene name='91/916397/Cv/7'>D2 small domain</scene>. The <scene name='91/916397/Cv/8'>first nucleotide AMPPNP binding site</scene> at NBD1 includes several hydrophobic residues as does the <scene name='91/916397/Cv/9'>second NBD</scene><ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.

	==ClpB 3D structures==		==ClpB 3D structures==

Alexander Berchansky at 11:32, 7 July 2022

Alexander Berchansky — Thu, 07 Jul 2022 11:32:48 GMT

←Older revision		Revision as of 11:32, 7 July 2022
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	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, first nucleotide-binding domain <scene name='91/916397/Cv/4'>(NBD1)</scene>, a long coiled-coil <scene name='91/916397/Cv/5'>linker</scene> domain, a <scene name='91/916397/Cv/6'>second NBD</scene> and a <scene name='91/916397/Cv/7'>D2 small domain</scene>. The first ~~NBD interacts with the~~ nucleotide AMPPNP ~~via 5~~ hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.	+	The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, first nucleotide-binding domain <scene name='91/916397/Cv/4'>(NBD1)</scene>, a long coiled-coil <scene name='91/916397/Cv/5'>linker</scene> domain, a <scene name='91/916397/Cv/6'>second NBD</scene> and a <scene name='91/916397/Cv/7'>D2 small domain</scene>. The <scene name='91/916397/Cv/8'>first nucleotide AMPPNP binding site</scene> at NBD1 includes several hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.

	==ClpB 3D structures==		==ClpB 3D structures==

Alexander Berchansky at 11:15, 7 July 2022

Alexander Berchansky — Thu, 07 Jul 2022 11:15:23 GMT

←Older revision		Revision as of 11:15, 7 July 2022
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	== Disease ==		== Disease ==

-	CLPb deficiency is a rare disorder characterized by neurological problems and shortage of white blood cells<ref>PMID:27891836</ref>.. ClpB mutations cause progressive brain atrophy<ref>PMID:25597510</ref>.	+	CLPb deficiency is a rare disorder characterized by neurological problems and shortage of white blood cells<ref>PMID:27891836</ref>. ClpB mutations cause progressive brain atrophy<ref>PMID:25597510</ref>.

	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, nucleotide-binding domain (~~NBD~~) 1, a long coiled-coil linker domain, a second NBD and a D2 small domain. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.	+	The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, first nucleotide-binding domain <scene name='91/916397/Cv/4'>(NBD1)</scene>, a long coiled-coil <scene name='91/916397/Cv/5'>linker</scene> domain, a <scene name='91/916397/Cv/6'>second NBD</scene> and a <scene name='91/916397/Cv/7'>D2 small domain</scene>. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.

	==ClpB 3D structures==		==ClpB 3D structures==

Alexander Berchansky at 11:04, 7 July 2022

Alexander Berchansky — Thu, 07 Jul 2022 11:04:16 GMT

←Older revision		Revision as of 11:04, 7 July 2022
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	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of ClpB ~~hexameric~~ complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: N-terminal, nucleotide-binding domain (NBD) 1, a long coiled-coil linker domain, a second NBD and a D2 small domain. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.	+	The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, nucleotide-binding domain (NBD) 1, a long coiled-coil linker domain, a second NBD and a D2 small domain. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.

	==ClpB 3D structures==		==ClpB 3D structures==

Alexander Berchansky at 12:30, 6 July 2022

Alexander Berchansky — Wed, 06 Jul 2022 12:30:51 GMT

←Older revision		Revision as of 12:30, 6 July 2022
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-	<StructureSection load='1qvr' size='340' side='right' caption='Thermus thermophilus ClpB complex with AMPPNP (PDB ID [[1qvr]])' scene=''>	+	<StructureSection load='1qvr' size='340' side='right' caption='Thermus thermophilus ClpB complex with AMPPNP (PDB ID [[1qvr]])' scene='91/916397/Cv/2'>

	== Function ==		== Function ==

Michal Harel at 09:31, 4 July 2022

Michal Harel — Mon, 04 Jul 2022 09:31:35 GMT

←Older revision		Revision as of 09:31, 4 July 2022
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	== Disease ==		== Disease ==

-	~~== Relevance ==~~	+	CLPb deficiency is a rare disorder characterized by neurological problems and shortage of white blood cells<ref>PMID:27891836</ref>.. ClpB mutations cause progressive brain atrophy<ref>PMID:25597510</ref>.

	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of ClpB complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: N-terminal, nucleotide-binding domain (NBD) 1, a long coiled-coil linker domain, a second NBD and a D2 small domain. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>.	+	The 3D structure of ClpB hexameric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: N-terminal, nucleotide-binding domain (NBD) 1, a long coiled-coil linker domain, a second NBD and a D2 small domain. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.
		+
		+	==ClpB 3D structures==
		+	[[3D structures of ClpB]]

	</StructureSection>		</StructureSection>

Michal Harel at 09:15, 4 July 2022

Michal Harel — Mon, 04 Jul 2022 09:15:42 GMT

←Older revision		Revision as of 09:15, 4 July 2022
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	== Structural highlights ==		== Structural highlights ==

-		+	The 3D structure of ClpB complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: N-terminal, nucleotide-binding domain (NBD) 1, a long coiled-coil linker domain, a second NBD and a D2 small domain. The first NBD interacts with the nucleotide AMPPNP via 5 hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>.

	</StructureSection>		</StructureSection>

Michal Harel at 08:55, 4 July 2022

Michal Harel — Mon, 04 Jul 2022 08:55:43 GMT

←Older revision		Revision as of 08:55, 4 July 2022
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-	<StructureSection load='1qvr' size='340' side='right' caption='Thermus thermophilus ClpB (~~PDD~~ ID [[1qvr]])' scene=''>	+	<StructureSection load='1qvr' size='340' side='right' caption='Thermus thermophilus ClpB complex with AMPPNP (PDB ID [[1qvr]])' scene=''>

	== Function ==		== Function ==

Michal Harel at 08:54, 4 July 2022

Michal Harel — Mon, 04 Jul 2022 08:54:06 GMT

←Older revision		Revision as of 08:54, 4 July 2022
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-	<StructureSection load='1qvr' size='340' side='right' caption='~~Caption for this structure~~' scene=''>	+	<StructureSection load='1qvr' size='340' side='right' caption='Thermus thermophilus ClpB (PDD ID [[1qvr]])' scene=''>
-	~~This is a default text for your page '''Chaperone protein ClpB'''. 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 ==		== Function ==
		+
		+	'''Chaperone protein ClpB''' (ClpB) reactivates aggregated proteins in cooperation with Hsp70<ref>PMID:24843029</ref>. ClpB is an ATP-dependent chaperone which can rescue proteins from an aggregated state.

	== Disease ==		== Disease ==
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	== Structural highlights ==		== 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>		</StructureSection>