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[edit]
- ^ a b Wu HY, Liu MS, Lin TP, Cheng YS (November 2011). "Structural and functional assays of AtTLP18.3 identify its novel acid phosphatase activity in thylakoid lumen". Plant Physiology. 157 (3): 1015–25. doi:10.1104/pp.111.184739. PMC 3252143. PMID 21908686.
- ^ a b Eletsky A, Acton TB, Xiao R, Everett JK, Montelione GT, Szyperski T (March 2012). "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. doi:10.1007/s10969-011-9122-2. PMC 3609422. PMID 22198206.
- ^ Sirpiö S, Allahverdiyeva Y, Suorsa M, Paakkarinen V, Vainonen J, Battchikova N, Aro EM (September 2007). "TLP18.3, a novel thylakoid lumen protein regulating photosystem II repair cycle". The Biochemical Journal. 406 (3): 415–25. doi:10.1042/BJ20070460. PMC 2049043. PMID 17576201.
- ^ Boulin T, Rapti G, Briseño-Roa L, Stigloher C, Richmond JE, Paoletti P, Bessereau JL (October 2012). "Positive modulation of a Cys-loop acetylcholine receptor by an auxiliary transmembrane subunit". Nature Neuroscience. 15 (10): 1374–81. doi:10.1038/nn.3197. PMID 22922783. S2CID 1282719.