Rossmann fold: Difference between revisions
Interactive scenes for ferredoxin reductase |
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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. | ||
==A βαβ fold example in ferredoxin reductase == | |||
To illustrate a βαβ fold in a complete protein an example is shown in Figure 4. 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. | |||
<Structure load='1f3p' size='500' frame='true' align='right' caption='FAD bindings site of ferredoxin reductase. PDB ID: 1F3P.' scene='59/595757/Ferredoxin-reductase-fad/2' /> | |||
The two core β-strand of the enzyme are shown in cyan colored "rocket" format, with a red colored helix in between the two strands. | |||
==Extension of the beta sheet by additional strands== | ==Extension of the beta sheet by additional strands== | ||