Three-dimensional (3D) structures of soybean and chickpea CMT and MET proteins constructed by homology modeling.

<p>(A) Ribbon representation of GmCMT2 and CaCMT2 protein structures with bound H3(1–32)K9me2 peptide. The BAH, methyltransferase, and Chr domains are colored in red, cyan, and blue, respectively, with bound S-adenosylhomocysteine (SAH) molecule (orange) and H3(1–32)K9me2 peptide (yellow, bound to BAH domain) shown in a space filling representation. <i>Inset</i> shows K9me2 accommodated within an aromatic cage formed by Tyr115, Tyr138 and Trp136 in GmCMT2 and by Tyr149, Tyr174 and Trp170 in CaCMT2. (B) Ribbon representation of homology modeled GmMET2 and CaMET1. The RFD, BAH and methyltransferase domains are colored in magenta, blue, and cyan, respectively. The K9me2 is accommodated within an aromatic cage in BAH1 of GmMET2 and in BAH1 of CaMET1 (<i>Inset</i>).