Rossmann fold: Difference between revisions
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NAD(P) is a two electron acceptor and donates the two electrons to FAD. The transfer of electrons takes place from C4 of NAD(P) to N5 of FAD. Each of these atoms is marked by its respective number in Figure 1. | NAD(P) is a two electron acceptor and donates the two electrons to FAD. The transfer of electrons takes place from C4 of NAD(P) to N5 of FAD. Each of these atoms is marked by its respective number in Figure 1. | ||
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==Contact region between Rossmann fold and FAD== | ==Contact region between Rossmann fold and FAD== | ||
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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. | 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. | ||
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==Contact region between Rossmann fold and NAD(P)== | ==Contact region between Rossmann fold and NAD(P)== | ||
[[Image:NAD-binding-sites.png|500px|right|thumb| Fig. 3. NAD binding sites of 3-phosphoglycerate dehydrogenase ([[2p9e]]) (residues 152-182) and lactate dehydrogenase ([[1ioz]]). NAD is shown in CPK mode.]] | [[Image:NAD-binding-sites.png|500px|right|thumb| Fig. 3. NAD binding sites of 3-phosphoglycerate dehydrogenase ([[2p9e]]) (residues 152-182) and lactate dehydrogenase ([[1ioz]]). NAD is shown in CPK mode.]] | ||
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The βαβ fold has a structure similar to the fold shown above for FAD. For both enzymes, the first β-strand is followed by a tight turn that is connected to the N-terminal of the helix. The same Gly-x-Gly-x-x-Gly consensus sequence appears at the turn between the first strand and the helix. Again, similar to FAD site, the turn region is in contact with the negatively charged oxygens (red colored) of the two phosphate (orange colored) groups. | The βαβ fold has a structure similar to the fold shown above for FAD. For both enzymes, the first β-strand is followed by a tight turn that is connected to the N-terminal of the helix. The same Gly-x-Gly-x-x-Gly consensus sequence appears at the turn between the first strand and the helix. Again, similar to FAD site, the turn region is in contact with the negatively charged oxygens (red colored) of the two phosphate (orange colored) groups. | ||
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==A βαβ fold example in ferredoxin reductase == | ==A βαβ fold example in ferredoxin reductase == | ||
