Rossmann fold: Difference between revisions
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Figure 3 shows the Rossmann fold of two NAD binding proteins, 3-phosphoglycerate dehydrogenase ([[2p9e]])<ref>PMID:17459882</ref> and lactate dehydrogenase ([[1i0z]]) (residues 21-53) <ref>PMID:11276087</ref>. In enzymes that have just an NAD binding site, the site may be close to the N terminus of the protein as in lactate dehydrogenase. In flavoproteins that bind two dinucleotides, such as glutathione reductase and adrenodoxin reductase <ref name="HI-1989" />, the NAD(P) binding site appears in the middle of the protein. | Figure 3 shows the Rossmann fold of two NAD binding proteins, 3-phosphoglycerate dehydrogenase ([[2p9e]])<ref>PMID:17459882</ref> and lactate dehydrogenase ([[1i0z]]) (residues 21-53) <ref>PMID:11276087</ref>. In enzymes that have just an NAD binding site, the site may be close to the N terminus of the protein as in lactate dehydrogenase. In flavoproteins that bind two dinucleotides, such as glutathione reductase and adrenodoxin reductase <ref name="HI-1989" />, the NAD(P) binding site appears in the middle of the protein. | ||
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 | 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 <span style="color:red">oxygens</span> of the two <span style="color:DarkOrange">phosphate</span> groups. | ||
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