NMR Structural Study of phytochrome B PAS1 and PAS2 domain

Abstract

PAS (PER-ARNT-SIM) domain, found in diverse proteins throughout all three kingdoms of life, is a family of sensor protein domains that mediate protein-protein interactions or bind small ligands and/or cofactors. It is interesting that these domains contain a structurally conserved α/β -fold, whereas low sequence similarity is observed. There are two PAS domains in plant photoreceptor phytochromes and its roles for phototransformation have been demonstrated by genetical approach in Arabidopsis. In this research, we have attempted to determine the solution structure of the rice phytochrome B PAS domain (L806-A923) by using multidimensional NMR spectroscopy to discuss structure and function relationship. To date, by analyses of secondary structure, rice phytochrome B PAS domain possess typical PAS fold.