Rossmann fold: Difference between revisions

Added links to PDB codes
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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.]]
Figure 3 shows the Rossmann fold of two NAD binding proteins, 3-phosphoglycerate dehydrogenase ([[2p9e]])<ref>PMID:17459882</ref> and lactate dehydrogenase ([[1ioz]]) (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 &beta;&alpha;&beta; fold has a structure similar to the fold shown above for FAD.  For both enzymes, the first &beta;-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 &beta;&alpha;&beta; fold has a structure similar to the fold shown above for FAD.  For both enzymes, the first &beta;-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.


==A &beta;&alpha;&beta; fold example in ferredoxin reductase ==
==A &beta;&alpha;&beta; fold example in ferredoxin reductase ==

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