Biology:TPM domain
| TPM domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | TPM | ||||||||
| Pfam | PF04536 | ||||||||
| InterPro | IPR007621 | ||||||||
| |||||||||
The TPM domain family is named after the three founding proteins TLP18.3, Psb32 and MOLO-1. TPM domains have a characteristic fold (αβαβαββαα[1] or βαβαββαα[2]) composed of α helices (3+3[1] or 2+3[2]) 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 have been implicated 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 the model nematode C. elegans, the MOLO-1 protein is an auxiliary subunit that positively modulates the gating of levamisole-sensitive acetylcholine receptors.[4]
References
- ↑ 1.0 1.1 "Structural and functional assays of AtTLP18.3 identify its novel acid phosphatase activity in thylakoid lumen". Plant Physiology 157 (3): 1015–25. November 2011. doi:10.1104/pp.111.184739. PMID 21908686.
- ↑ 2.0 2.1 "Solution NMR structures reveal a distinct architecture and provide first structures for protein domain family PF04536". Journal of Structural and Functional Genomics 13 (1): 9–14. March 2012. doi:10.1007/s10969-011-9122-2. PMID 22198206.
- ↑ "TLP18.3, a novel thylakoid lumen protein regulating photosystem II repair cycle". The Biochemical Journal 406 (3): 415–25. September 2007. doi:10.1042/BJ20070460. PMID 17576201.
- ↑ "Positive modulation of a Cys-loop acetylcholine receptor by an auxiliary transmembrane subunit". Nature Neuroscience 15 (10): 1374–81. October 2012. doi:10.1038/nn.3197. PMID 22922783.
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