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Function

Mhp1 is a transmembrane protein bellowing to the nucleobase-cation-symport-1 (NCS1) transporter family from Microbacterium liquefaciens. It allows the sodium dependent income of indolyl methyl- and benzyl-hydantoins in the cell. Those are part of a salvage metabolic pathway leading to their conversion in amino acids.

Figure 1 : Structure of benzyl-hydantoin

Disease

Relevance

Structural highlights

Global stucture

The protein is composed of one chain of 12 transmembrane alpha helices (TMs). They are organised in two repeating units connected by a 59-residue loop (TMs 1-5 and TMs 6-10) and two additional helices (TM 11 and 12). The two repeating units have a symmetrical topology (Figure 2).

Figure 2 : Structure of Mhp1 from Microbacterum liquefaciens

The central bundle is composed of TMs 1 and 2, twined to the TMs 6 and 7 respectively. In addition, the protein presents a V-shape structure formed by TMs 3 to 5, twined to TMs 8 to 10 (Figure 2.A).

The substrate- and cation-binding sites are located in the space between the central four-helix-bundle and the outer helix layer.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.