BA42: Difference between revisions

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==BA42 Protein from ''Bizionia argentinensis''==

<StructureSection load='' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with Ca2+

ions (PDB code [[4oa3]])' scene='71/715464/Cv/1'>

== Function ==

Unknown

~~== Disease ==~~

NA

== Relevance ==

Protein phosphatase from ''Bizionia argentinensis''

== 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<ref>pmid 21908686~~</~~ref~~> or βαβαββαα~~<ref>pmid 22198206~~</~~ref~~>) 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 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>

~~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.~~

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

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

</StructureSection>

== 3D structure of BA42 ==

[[2lt2]], [[2mpb]] - BaBA42 - ''Bizonia argentinesis'' - NMR<br />

[[4oa3]] - BaBA42<br />

== References ==

[[Category:Topic Page]]

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@@ Line 1: / Line 1: @@
 ==BA42 Protein from ''Bizionia argentinensis''==
-<StructureSection load='4oa3' size='512' side='right' caption='Deoxyribose-phosphate aldolase complex with acetate (PDB code [[4oa3]])' scene=''>
+<StructureSection load='' size='400' side='right' caption='Antarctic bacterium protein BA42 complex with Ca2+
+ ions (PDB code [[4oa3]])' scene='71/715464/Cv/1'>
 == Function ==
 Unknown
-== Disease ==
-NA
 == Relevance ==
 Protein phosphatase from ''Bizionia argentinensis''
 == 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<ref>pmid 21908686</ref> or βαβαββαα<ref>pmid 22198206</ref>) 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 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>
-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.
+<scene name='71/715464/Cv/7'>1st Ca2+ coordination site</scene>. Water molecules sre shown as red spheres.
+<scene name='71/715464/Cv/8'>2nd Ca2+ coordination site</scene> in Antarctic bacterium protein BA42 (PDB code [[4oa3]]).<ref>PMID:25116514</ref>
 </StructureSection>
+== 3D structure of BA42 ==
+[[2lt2]], [[2mpb]] - BaBA42 - ''Bizonia argentinesis'' - NMR<br />
+[[4oa3]] - BaBA42<br />
 == References ==
 <references/>
+[[Category:Topic Page]]