BA42: Difference between revisions
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==BA42 Protein from ''Bizionia argentinensis''== | ==BA42 Protein from ''Bizionia argentinensis''== | ||
<StructureSection load=' | <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'> | ||
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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/ | '''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> | ||
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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/ | <scene name='71/715464/Cv/7'>1st Ca2+ coordination site</scene>. Water molecules sre shown as red spheres. | ||
<scene name='71/715464/Cv/ | <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> | ||
== 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]] | |||
Latest revision as of 07:29, 24 October 2022
BA42 Protein from Bizionia argentinensis
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3D structure of BA42
4oa3, 2mpb - BaBA42 - Bizonia argentinesis - NMR
4oa3 - BaBA42
References
Proteopedia Page Contributors and Editors (what is this?)
Martin Aran, Alexander Berchansky, Joel L. Sussman, Michal Harel
