BA42: Difference between revisions

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

~~This is a default text for your page '''BA42 Protein from Bizionia argentinensis'''. 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>10.1002/prot.24667</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.~~

== Function ==

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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 or βαβαββαα) composed of α helices (3+3 or 2+3) 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 (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".

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.~~[3]~~

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 ~~12345~~</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.

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 ==BA42 Protein from ''Bizionia argentinensis''==
 <StructureSection load='4oa3' size='512' side='right' caption='Caption for this structure' scene=''>
-This is a default text for your page '''BA42 Protein from Bizionia argentinensis'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
-You may include any references to papers as in: the use of JSmol in Proteopedia <ref>10.1002/prot.24667</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 == Function ==
@@ Line 11: / Line 9: @@
 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 or βαβαββαα) composed of α helices (3+3 or 2+3) 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 (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".
-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.[3]
+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 12345</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.