ADP-ribose pyrophosphatase - Revision history

Michal Harel at 09:31, 9 March 2021

Michal Harel — Tue, 09 Mar 2021 09:31:57 GMT

←Older revision		Revision as of 09:31, 9 March 2021
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	== Function ==		== Function ==

-	'''ADP-ribose pyrophosphatase''' (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.<ref>PMID:11323725</ref> ADPRP belongs to the family of NUDIX hydrolase.	+	'''ADP-ribose pyrophosphatase''' (ADPRP) or '''ADPRase''' catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.<ref>PMID:11323725</ref> ADPRP belongs to the family of NUDIX hydrolase.

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

Michal Harel at 07:19, 1 June 2020

Michal Harel — Mon, 01 Jun 2020 07:19:53 GMT

←Older revision		Revision as of 07:19, 1 June 2020
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	<StructureSection load='1khz' size='450' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'>		<StructureSection load='1khz' size='450' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'>
-		+	__TOC__
	== Function ==		== Function ==

Michal Harel at 09:04, 3 March 2019

Michal Harel — Sun, 03 Mar 2019 09:04:24 GMT

←Older revision		Revision as of 09:04, 3 March 2019
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	</StructureSection>		</StructureSection>
-	==3D structures of ADP-ribose pyrophosphatase==

-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*ADP-ribose pyrophosphatase
-
-	**[[1q33]] – hADPRP NUDT9 residues 59-350 – human<br />
-	**[[1v8i]], [[3x0i]], [[3x0j]], [[3x0l]], [[3x0n]], [[3x0p]], [[3x0q]], [[3x0s]] - TtADPRP – ''Thermus thermophilus''<br />
-	**[[3x0k]], [[3k0l]] - TtADPRP ES-state <br />
-	**[[3x0m]], [[3k0n]] - TtADPRP ESM-state <br />
-	**[[3x0o]], [[3k0p]], [[3k0q]] - TtADPRP ESMM-state <br />
-	**[[3x0r]], [[3k0s]] - TtADPRP E'-state <br />
-	**[[2w4e]] – ADPRP residues 56-200 – ''Deinococcus radiodurans''<br />
-	**[[3o8s]] - ADPRP – ''Streptococcus suis''<br />
-	**[[4kyx]] – ADPRP Mutt – ''Rickettsia felis''<br />
-	**[[5i8u]] - ADPRP – ''Mycobacterium tuberculosis''<br />
-	**[[1viq]], [[1viu]] - EcADPRP – ''Escherichia coli''<br />
-
-	*ADP-ribose pyrophosphatase binary complex
-
-	**[[1v8l]] – TtADPRP + ADPR<br />
-	**[[1v8n]] - TtADPRP + Zn<br />
-
-	*ADP-ribose pyrophosphatase ternary complex
-
-	**[[1khz]] - EcADPRP + AMPCPR + Mg <br />
-	**[[1qvj]] - hADPRP + ribose-5-phosphate + Mg<br />
-	**[[1v8m]] - TtADPRP + Gd + ADPR <br />
-	**[[1v8s]] - TtADPRP + AMP + Mg<br />
-	**[[1v8t]] - TtADPRP + ribose-5-phosphate + Zn<br />
-	**[[1v8u]] - TtADPRP (mutant) + sulfate + Mg<br />
-	**[[1v8v]] - TtADPRP (mutant) + ADPR + Mg<br />
-	**[[1v8w]] - TtADPRP (mutant) + sulfate + Zn<br />
-	**[[1v8y]] - TtADPRP (mutant) + ADPR + Zn<br />
-	**[[1v8r]] - TtADPRP + ADPR + Zn<br />
-	**[[3bm4]] - hADPRP NUDT5 + AMPCPR + Mg<br />
-	}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 09:03, 3 March 2019

Michal Harel — Sun, 03 Mar 2019 09:03:22 GMT

←Older revision		Revision as of 09:03, 3 March 2019
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	==3D structures of ADP-ribose pyrophosphatase==		==3D structures of ADP-ribose pyrophosphatase==
-	[[ADP-ribose pyrophosphatase	+
		+	[[ADP-ribose pyrophosphatase 3D structures]]

	</StructureSection>		</StructureSection>

Michal Harel at 09:02, 3 March 2019

Michal Harel — Sun, 03 Mar 2019 09:02:29 GMT

←Older revision		Revision as of 09:02, 3 March 2019
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	== Function ==		== Function ==

-	'''ADP-ribose pyrophosphatase''' (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.<ref>PMID:11323725</ref> ADPRP belongs to the family of [[NUDIX hydrolase]].	+	'''ADP-ribose pyrophosphatase''' (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.<ref>PMID:11323725</ref> ADPRP belongs to the family of NUDIX hydrolase.

	== Structural highlights ==		== Structural highlights ==
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	*<scene name='48/488514/Cv/18'>2nd Mg+2 ion coordination site</scene>.		*<scene name='48/488514/Cv/18'>2nd Mg+2 ion coordination site</scene>.
	*<scene name='48/488514/Cv/19'>3rd Mg+2 ion coordination site</scene>.		*<scene name='48/488514/Cv/19'>3rd Mg+2 ion coordination site</scene>.
		+
		+	==3D structures of ADP-ribose pyrophosphatase==
		+	[[ADP-ribose pyrophosphatase
		+
	</StructureSection>		</StructureSection>
	==3D structures of ADP-ribose pyrophosphatase==		==3D structures of ADP-ribose pyrophosphatase==

Alexander Berchansky at 11:22, 26 December 2018

Alexander Berchansky — Wed, 26 Dec 2018 11:22:31 GMT

←Older revision		Revision as of 11:22, 26 December 2018
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	ADPRP contains two domains: the <scene name='48/488514/Cv/9'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site. The C-terminal domain contains the <scene name='48/488514/Cv/10'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/15'>Residues from both monomers of ADPRP participate in the active site</scene>.<ref>PMID:12135348</ref> Water molecules are shown as red spheres.		ADPRP contains two domains: the <scene name='48/488514/Cv/9'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site. The C-terminal domain contains the <scene name='48/488514/Cv/10'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/15'>Residues from both monomers of ADPRP participate in the active site</scene>.<ref>PMID:12135348</ref> Water molecules are shown as red spheres.
		+	*<scene name='48/488514/Cv/16'>Interactions of Mg+2 ion cluster</scene>.
		+	*<scene name='48/488514/Cv/17'>1st Mg+2 ion coordination site</scene>.
		+	*<scene name='48/488514/Cv/18'>2nd Mg+2 ion coordination site</scene>.
		+	*<scene name='48/488514/Cv/19'>3rd Mg+2 ion coordination site</scene>.
	</StructureSection>		</StructureSection>
	==3D structures of ADP-ribose pyrophosphatase==		==3D structures of ADP-ribose pyrophosphatase==

Alexander Berchansky at 11:16, 26 December 2018

Alexander Berchansky — Wed, 26 Dec 2018 11:16:59 GMT

←Older revision		Revision as of 11:16, 26 December 2018
Line 7:		Line 7:
	== Structural highlights ==		== Structural highlights ==

-	ADPRP contains two domains: the <scene name='48/488514/Cv/9'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site. The C-terminal domain contains the <scene name='48/488514/Cv/10'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/15'>Residues from both monomers of ADPRP participate in the active site</scene>.<ref>PMID:12135348</ref>	+	ADPRP contains two domains: the <scene name='48/488514/Cv/9'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site. The C-terminal domain contains the <scene name='48/488514/Cv/10'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/15'>Residues from both monomers of ADPRP participate in the active site</scene>.<ref>PMID:12135348</ref> Water molecules are shown as red spheres.
	</StructureSection>		</StructureSection>
	==3D structures of ADP-ribose pyrophosphatase==		==3D structures of ADP-ribose pyrophosphatase==

Alexander Berchansky at 11:16, 26 December 2018

Alexander Berchansky — Wed, 26 Dec 2018 11:16:04 GMT

←Older revision		Revision as of 11:16, 26 December 2018
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-	<StructureSection load='1khz' size='~~350~~' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'>	+	<StructureSection load='1khz' size='450' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'>

	== Function ==		== Function ==

Alexander Berchansky at 11:15, 26 December 2018

Alexander Berchansky — Wed, 26 Dec 2018 11:15:27 GMT

←Older revision		Revision as of 11:15, 26 December 2018
Line 7:		Line 7:
	== Structural highlights ==		== Structural highlights ==

-	ADPRP contains two domains: the <scene name='48/488514/Cv/9'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site. The C-terminal domain contains the <scene name='48/488514/Cv/10'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/11'>Residues from both monomers of ADPRP participate in the active site</scene>.<ref>PMID:12135348</ref>	+	ADPRP contains two domains: the <scene name='48/488514/Cv/9'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site. The C-terminal domain contains the <scene name='48/488514/Cv/10'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/15'>Residues from both monomers of ADPRP participate in the active site</scene>.<ref>PMID:12135348</ref>
	</StructureSection>		</StructureSection>
	==3D structures of ADP-ribose pyrophosphatase==		==3D structures of ADP-ribose pyrophosphatase==

Michal Harel at 21:14, 13 September 2018

Michal Harel — Thu, 13 Sep 2018 21:14:55 GMT

←Older revision		Revision as of 21:14, 13 September 2018
Line 3:		Line 3:
	== Function ==		== Function ==

-	'''ADP-ribose pyrophosphatase''' (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.<ref>PMID:11323725</ref>	+	'''ADP-ribose pyrophosphatase''' (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.<ref>PMID:11323725</ref> ADPRP belongs to the family of [[NUDIX hydrolase]].

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