Rossmann fold: Difference between revisions
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==A βαβ fold example in ferredoxin reductase == | ==A βαβ fold example in ferredoxin reductase == | ||
To illustrate a βαβ fold in a complete protein | To illustrate a βαβ fold in a complete protein a 3D example is shown below. The example protein is a ferredoxin reductase from Pseudomonas that binds both an FAD and NADH <ref>PMID:11090282</ref>. This enzyme binds NADH which transfers its two electrons to the FAD coenzyme of ferredoxin reductase. These electrons are then transferred to a ferredoxin that is an iron sulfur electron transfer protein. This ferredoxin then donates the electrons to an oxygenase that uses the electrons in a dioxygenase reaction. | ||
The two core β-strands of the enzyme are shown in cyan colored "rocket" format, with a red colored helix in between the two strands. | The two core β-strands of the enzyme are shown in cyan colored "rocket" format, with a red colored helix in between the two strands. | ||
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<scene name='59/595757/Ferredoxin-reductase-fad-gly14/2'>Click here to see the first conserved glycine in space filling CPK format at the end of the first beta-strand.</scene> | <scene name='59/595757/Ferredoxin-reductase-fad-gly14/2'>Click here to see the first conserved glycine in space filling CPK format at the end of the first beta-strand.</scene> | ||
<scene name='59/595757/Ferredoxin-reductase-fad-gly16/ | <scene name='59/595757/Ferredoxin-reductase-fad-gly16/4'>Click here to see the second conserved glycine in space filling CPK format at the beginning of the helix.</scene> | ||
<scene name='59/595757/Ferredoxin-reductase-fad-5-78/1'>Click here to see the structure of the residues 5-78.</scene> Note that in between the second β-strand and the third one there are four α-helical segments. | <scene name='59/595757/Ferredoxin-reductase-fad-5-78/1'>Click here to see the structure of the residues 5-78.</scene> Note that in between the second β-strand and the third one there are four α-helical segments. | ||