Rossmann fold: Difference between revisions
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==Contact region between Rossmann fold and FAD== | ==Contact region between Rossmann fold and FAD== | ||
[[Image:FAD-binding-sites.png|500px|right|thumb| Fig. 2. FAD binding sites of D-amino acid oxidase (2E48) (residues 1-36) and glutathione reductase (3GRS) (residues 21-50). FAD is shown in CPK mode.]] | [[Image:FAD-binding-sites.png|500px|right|thumb| Fig. 2. The FAD binding sites of D-amino acid oxidase (2E48) (residues 1-36) and glutathione reductase (3GRS) (residues 21-50). FAD is shown in CPK mode.]] | ||
In dinucleotide binding flavoproteins, FAD binding Rossmann fold is commonly located close to the amino terminus of the protein. Figure 2 shows the first Rossmann fold of two flavoproteins, D-amino acid oxidase (2e48)<ref>PMID:17303072</ref> and glutathione reductase (3GRS)<ref>PMID:3656429</ref>. In both enzymes, the first β-strand is followed by a tight loop that is connected to the N-terminal of the helix. The two highly conserved Gly residues in the consensus sequence are located in this turn to allow the sharp bending of the chain. At the end of the helix there is a wider turn that is followed by the second beta strand that runs parallel to the first strand. | In dinucleotide binding flavoproteins, FAD binding Rossmann fold is commonly located close to the amino terminus of the protein. Figure 2 shows the first Rossmann fold of two flavoproteins, D-amino acid oxidase (2e48)<ref>PMID:17303072</ref> and glutathione reductase (3GRS)<ref>PMID:3656429</ref>. In both enzymes, the first β-strand is followed by a tight loop that is connected to the N-terminal of the helix. The two highly conserved Gly residues in the consensus sequence are located in this turn to allow the sharp bending of the chain. At the end of the helix there is a wider turn that is followed by the second beta strand that runs parallel to the first strand. | ||
FAD structure is shown in CPK format. The atoms can be identified by their colors: C: grey; O: red, P: orange and N: purple. The turn at β-α border is in contact with the negatively charged oxygens (red colored) of the two phosphate (orange colored) groups. | The FAD structure is shown in CPK format. The atoms can be identified by their colors: C: grey; O: red, P: orange and N: purple. The turn at β-α border is in contact with the negatively charged oxygens (red colored) of the two phosphate (orange colored) groups. | ||
==Contact region between Rossmann fold and NAD(P)== | ==Contact region between Rossmann fold and NAD(P)== | ||