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 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. | To illustrate a βαβ fold in a complete protein, a 3D example (PDB ID: 1F3P) 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. | ||
Below the two core β-strands of the enzyme (PDB ID: 1F3P) are shown in cyan colored "rocket" format, with a red colored helix in between the two strands. | |||
<Structure load='1f3p' size='500' frame='false' align='right' caption='Fig. 4. FAD binding site of ferredoxin reductase. PDB ID: 1F3P.' scene='59/595757/Ferredoxin-reductase-fad/2' /> | <Structure load='1f3p' size='500' frame='false' align='right' caption='Fig. 4. FAD binding site of ferredoxin reductase. PDB ID: 1F3P.' scene='59/595757/Ferredoxin-reductase-fad/2' /> | ||
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<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. | ||
<scene name='59/595757/Ferredoxin-reductase-full/3'>Click here to see the full structure of ferredoxin reductase.</scene> Note that FAD has been colored a yellowish green, and NADP is shown also in CPK format that neighbors FAD. | |||
==Extension of the beta sheet by additional strands== | ==Extension of the beta sheet by additional strands== | ||
[[Image:3-phosphoglycerate_dehydrogenase-2P9E-sheet.png|400px|right|thumb| Fig. | [[Image:3-phosphoglycerate_dehydrogenase-2P9E-sheet.png|400px|right|thumb| Fig. 5. 3-phosphoglycerate dehydrogenase (2P9E) beta sheet in the NAD binding domain. The two beta-strands that form the core of the Rossmann fold are marked in dark-blue color.]] | ||
In many (but not all) proteins with βαβ fold, the β-strands may be part of a larger β-sheet with up to seven β-strands. Figure 4 shows five strands forming a β-sheet in phosphoglycerate dehydrogenase (2P9E). Note that the segment connecting the second strand to the third is in coiled confirmation and not helical. Whereas the subsequent connections between strands include α-helix segments. | As seen in the above example of ferredoxin reductase the β-sheet that is in the nucleotide domain may have more than two strands. In many (but not all) proteins with βαβ fold, the β-strands may be part of a larger β-sheet with up to seven β-strands. Figure 4 shows five strands forming a β-sheet in phosphoglycerate dehydrogenase (2P9E). Note that the segment connecting the second strand to the third is in coiled confirmation and not helical. Whereas the subsequent connections between strands include α-helix segments. | ||
==Evolutionary origin of the βαβ fold == | ==Evolutionary origin of the βαβ fold == | ||