BA42 - Revision history

Michal Harel at 07:29, 24 October 2022

Michal Harel — Mon, 24 Oct 2022 07:29:37 GMT

←Older revision		Revision as of 07:29, 24 October 2022
Line 21:		Line 21:
	== 3D structure of BA42 ==		== 3D structure of BA42 ==

-	[[2mpb]] - BaBA42 - ''Bizonia argentinesis'' - NMR<br />	+	[[2lt2]], [[2mpb]] - BaBA42 - ''Bizonia argentinesis'' - NMR<br />
	[[4oa3]] - BaBA42<br />		[[4oa3]] - BaBA42<br />
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Alexander Berchansky at 11:10, 7 January 2019

Alexander Berchansky — Mon, 07 Jan 2019 11:10:55 GMT

←Older revision		Revision as of 11:10, 7 January 2019
Line 8:		Line 8:
	Protein phosphatase from ''Bizionia argentinensis''		Protein phosphatase from ''Bizionia argentinensis''
	== Structural highlights ==		== Structural highlights ==
-	'''BA42''' belongs to the TPM protein family from Pfam. The TPM domain family is named after the three founding proteins TLP18.3, Psb32 and MOLO-1. TPM domains have a characteristic fold <scene name='71/715464/Cv/2'>(αβαβαββαα or βαβαββαα)</scene> composed of α helices (3+3<ref>pmid 21908686</ref> or 2+3<ref>pmid 22198206</ref>) flanking four central β strands. The TPM fold has not been found in other protein domains to date. TPM was previously referred to as "DUF477" and "Repair_PSII".	+	'''BA42''' belongs to the TPM protein family from Pfam. The TPM domain family is named after the three founding proteins TLP18.3, Psb32 and MOLO-1. TPM domains have a characteristic fold <scene name='71/715464/Cv/9'>(αβαβαββαα or βαβαββαα)</scene> composed of α helices (3+3<ref>pmid 21908686</ref> or 2+3<ref>pmid 22198206</ref>) flanking four central β strands. The TPM fold has not been found in other protein domains to date. TPM was previously referred to as "DUF477" and "Repair_PSII".

	In plants, the TPM domain-containing proteins TLP18.3 and Psb32 that have been implicated in the photosystem II (PSII) repair cycle. It may be involved in the regulation of synthesis/degradation of the D1 protein of the PSII core and in the assembly of PSII monomers into dimers in the grana stacks.<ref>pmid 17576201</ref>		In plants, the TPM domain-containing proteins TLP18.3 and Psb32 that have been implicated in the photosystem II (PSII) repair cycle. It may be involved in the regulation of synthesis/degradation of the D1 protein of the PSII core and in the assembly of PSII monomers into dimers in the grana stacks.<ref>pmid 17576201</ref>

Alexander Berchansky at 10:27, 17 May 2018

Alexander Berchansky — Thu, 17 May 2018 10:27:14 GMT

←Older revision		Revision as of 10:27, 17 May 2018
Line 14:		Line 14:
	In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>		In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>

-	<scene name='71/715464/Cv/4'>1st Ca2+ coordination site</scene>	+	<scene name='71/715464/Cv/7'>1st Ca2+ coordination site</scene>. Water molecules sre shown as red spheres.

-	<scene name='71/715464/Cv/6'>2nd Ca2+ coordination site</scene> in Antarctic bacterium protein BA42 (PDB code [[4oa3]]).<ref>PMID:25116514</ref>	+	<scene name='71/715464/Cv/8'>2nd Ca2+ coordination site</scene> in Antarctic bacterium protein BA42 (PDB code [[4oa3]]).<ref>PMID:25116514</ref>

	</StructureSection>		</StructureSection>

Joel L. Sussman at 11:56, 19 October 2017

Joel L. Sussman — Thu, 19 Oct 2017 11:56:05 GMT

←Older revision		Revision as of 11:56, 19 October 2017
Line 1:		Line 1:
	==BA42 Protein from ''Bizionia argentinensis''==		==BA42 Protein from ''Bizionia argentinensis''==
-	<StructureSection load='~~4oa3~~' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with Ca2+	+	<StructureSection load='' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with Ca2+
	ions (PDB code [[4oa3]])' scene='71/715464/Cv/1'>		ions (PDB code [[4oa3]])' scene='71/715464/Cv/1'>

Michal Harel at 20:42, 18 October 2017

Michal Harel — Wed, 18 Oct 2017 20:42:43 GMT

←Older revision		Revision as of 20:42, 18 October 2017
Line 25:		Line 25:
	== References ==		== References ==
	<references/>		<references/>
		+	[[Category:Topic Page]]

Alexander Berchansky at 13:40, 13 January 2016

Alexander Berchansky — Wed, 13 Jan 2016 13:40:52 GMT

←Older revision		Revision as of 13:40, 13 January 2016
Line 14:		Line 14:
	In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>		In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>

-	<scene name='71/715464/Cv/4'>1st Ca2+ ~~binding~~ site</scene>	+	<scene name='71/715464/Cv/4'>1st Ca2+ coordination site</scene>

-	<scene name='71/715464/Cv/6'>2nd Ca2+ ~~binding~~ site</scene> in Antarctic bacterium protein BA42 (PDB code [[4oa3]]).<ref>PMID:25116514</ref>	+	<scene name='71/715464/Cv/6'>2nd Ca2+ coordination site</scene> in Antarctic bacterium protein BA42 (PDB code [[4oa3]]).<ref>PMID:25116514</ref>

	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:09, 13 January 2016

Alexander Berchansky — Wed, 13 Jan 2016 12:09:17 GMT

←Older revision		Revision as of 12:09, 13 January 2016
Line 16:		Line 16:
	<scene name='71/715464/Cv/4'>1st Ca2+ binding site</scene>		<scene name='71/715464/Cv/4'>1st Ca2+ binding site</scene>

-	<scene name='71/715464/Cv/6'>2nd Ca2+ binding site</scene>	+	<scene name='71/715464/Cv/6'>2nd Ca2+ binding site</scene> in Antarctic bacterium protein BA42 (PDB code [[4oa3]]).<ref>PMID:25116514</ref>

	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:07, 13 January 2016

Alexander Berchansky — Wed, 13 Jan 2016 12:07:31 GMT

←Older revision		Revision as of 12:07, 13 January 2016
Line 1:		Line 1:
	==BA42 Protein from ''Bizionia argentinensis''==		==BA42 Protein from ''Bizionia argentinensis''==
-	<StructureSection load='4oa3' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with ~~Cl-~~ ions (PDB code [[4oa3]])' scene='71/715464/Cv/1'>	+	<StructureSection load='4oa3' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with Ca2+
		+	ions (PDB code [[4oa3]])' scene='71/715464/Cv/1'>

	== Function ==		== Function ==
Line 13:		Line 14:
	In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>		In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>

-	<scene name='71/715464/Cv/4'>1st Ca binding site</scene>	+	<scene name='71/715464/Cv/4'>1st Ca2+ binding site</scene>
		+
		+	<scene name='71/715464/Cv/6'>2nd Ca2+ binding site</scene>

	</StructureSection>		</StructureSection>

Alexander Berchansky at 11:36, 13 January 2016

Alexander Berchansky — Wed, 13 Jan 2016 11:36:27 GMT

←Older revision		Revision as of 11:36, 13 January 2016
Line 13:		Line 13:
	In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>		In the model nematode ''C. elegans'', the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.<ref>pmid 22922783</ref>

		+	<scene name='71/715464/Cv/4'>1st Ca binding site</scene>

	</StructureSection>		</StructureSection>

Alexander Berchansky at 11:09, 13 January 2016

Alexander Berchansky — Wed, 13 Jan 2016 11:09:04 GMT

←Older revision		Revision as of 11:09, 13 January 2016
Line 1:		Line 1:
	==BA42 Protein from ''Bizionia argentinensis''==		==BA42 Protein from ''Bizionia argentinensis''==
-	<StructureSection load='4oa3' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with Cl- ions (PDB code [[4oa3]])' scene=''>	+	<StructureSection load='4oa3' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with Cl- ions (PDB code [[4oa3]])' scene='71/715464/Cv/1'>

	== Function ==		== Function ==
Line 7:		Line 7:
	Protein phosphatase from ''Bizionia argentinensis''		Protein phosphatase from ''Bizionia argentinensis''
	== Structural highlights ==		== Structural highlights ==
-	'''BA42''' belongs to the TPM protein family from Pfam. The TPM domain family is named after the three founding proteins TLP18.3, Psb32 and MOLO-1. TPM domains have a characteristic fold (αβαβαββαα or βαβαββαα) composed of α helices (3+3<ref>pmid 21908686</ref> or 2+3<ref>pmid 22198206</ref>) flanking four central β strands. The TPM fold has not been found in other protein domains to date. TPM was previously referred to as "DUF477" and "Repair_PSII".	+	'''BA42''' belongs to the TPM protein family from Pfam. The TPM domain family is named after the three founding proteins TLP18.3, Psb32 and MOLO-1. TPM domains have a characteristic fold <scene name='71/715464/Cv/2'>(αβαβαββαα or βαβαββαα)</scene> composed of α helices (3+3<ref>pmid 21908686</ref> or 2+3<ref>pmid 22198206</ref>) flanking four central β strands. The TPM fold has not been found in other protein domains to date. TPM was previously referred to as "DUF477" and "Repair_PSII".

	In plants, the TPM domain-containing proteins TLP18.3 and Psb32 that have been implicated in the photosystem II (PSII) repair cycle. It may be involved in the regulation of synthesis/degradation of the D1 protein of the PSII core and in the assembly of PSII monomers into dimers in the grana stacks.<ref>pmid 17576201</ref>		In plants, the TPM domain-containing proteins TLP18.3 and Psb32 that have been implicated in the photosystem II (PSII) repair cycle. It may be involved in the regulation of synthesis/degradation of the D1 protein of the PSII core and in the assembly of PSII monomers into dimers in the grana stacks.<ref>pmid 17576201</ref>