Proline ligand-binding sites

Iron-sulfur clusters are important co-factors in electron-transfer. Type I reaction centres contain [4Fe-4S] clusters as final electron acceptors mediating ET to soluble electron carriers like ferredoxin or flavodoxin (reviewed in references 188, 224, 314, 315) In PS I three clusters (F FA and FB) have been clearly identified and spectroscopically characterized. The PsaA and PsaB subunits carry most of the ET cofactors in PS I.18178-316 Each of them provides two Cys ligands to the binding site of the interpolypeptide [4Fe-4S] cluster Fx. This binding site is identical on both core PS I subunits.317 Both [4Fe-4S] clusters FA and Fb are bound to the PS I stromal subunit PsaC. It contains two identical [4Fe-4S] consensus binding sites CxxCxxCxxxCP (C = cysteine, P = proline). 

The spectrin family of proteins, depending on the particular function, has numerous smaller motifs and binding sites for interaction with other proteins. These regions are important, as they are major protein-protein or protein-membrane interaction modules that bind to F-actin, proline-containing ligands, and/or phospholipids. Spectrin and dystrophin/utro-phin have all acquired copies of such domains since their evolution from a-actinin, presumably as a consequence of their more diverse roles in the cell. 

Table 1 Protein ligands that interact with the poly-l-proline-binding site of profiUn...

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