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Figure 1
The structure of apo wild-type MATα1. (a) The subunits of the wild-type MATα1 tetramer are shown in grey, green, yellow and blue. The tetramer is composed of two self-assembled dimers (four subunits of wild-type MATα1). (b) A homodimer is shown as blue and yellow ribbons. The gating loop (113–131) and residues 250–259 are shown in green and pink, respectively. The central part of the dimer interface is marked by a black square. Arg264 and Glu57 of each partner subunit form a salt bridge and stabilize dimer formation. (c) The interaction of Arg264 and Glu57 at the dimer interface is illustrated. Hydrogen bonds are represented by black dotted lines. The Arg264 and Glu57 residues of each subunit are labelled in different colours (blue and orange). (d, e) The active residues that interact with SAMe in the apo and SAMe-bound structures are shown as blue and pink sticks, respectively. The SAMe-bound structure was obtained from the Protein Data Bank (PDB entry 2obv). Hydrogen bonds are represented by black dotted lines.

Journal logoSTRUCTURAL
ISSN: 2059-7983
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