Rossmann fold: Difference between revisions
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Note: This entry on the Rossmann fold has been published in Biochem. Mol. Biol. Educ.<ref>PMID:25704928</ref>. Please cite it as Biochem. Mol. Biol. Educ. 43:206-209, 2015. | {{BAMBED | ||
|DATE=July 29, 2014 | |||
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|BAMBEDDOI=10.1002/bmb.20849 | |||
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Note: This entry on the Rossmann fold has been published in Biochem. Mol. Biol. Educ.<ref name="Hanukoglu-2015">PMID:25704928</ref>. Please cite it as Biochem. Mol. Biol. Educ. 43:206-209, 2015. | |||
The Rossmann fold is a super-secondary structure that is characterized by an alternating motif of beta-strand-alpha helix-beta strand secondary structures. Hence this fold is also called a βαβ fold. The β-strands participate in the formation of a β-sheet. The βαβ fold structure is commonly observed in enzymes that have dinucleotide coenzymes, such as FAD, NAD and NADP. | The Rossmann fold is a super-secondary structure that is characterized by an alternating motif of beta-strand-alpha helix-beta strand secondary structures. Hence this fold is also called a βαβ fold. The β-strands participate in the formation of a β-sheet. The βαβ fold structure is commonly observed in enzymes that have dinucleotide coenzymes, such as FAD, NAD and NADP. | ||
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The following scenes illustrate some aspects of the structure. | The following scenes illustrate some aspects of the structure. | ||
As noted above, the Rossmann fold is associated with a specific consensus sequence of Gly-x-Gly-x-x-Gly at the region of the tight loop between the first β-strand the α-helix. | |||
The first two scenes demonstrate the location of the first two conserved glycines. | |||
To rotate the molecule click and hold left mouse button. | To rotate the molecule click and hold left mouse button. | ||
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[[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 ( <span style="color:MediumBlue">██</span> )color.]] | [[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 ( <span style="color:MediumBlue">██</span> )color.]] | ||
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 5 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 5 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 example in Fig. 5, the direction of the strands are all parallel. This represents a general trend in Rossmann folds. However in some Rossmann folds there may be some strands in anti-parallel direction.<ref name="Hanukoglu-2015" /> | |||
As compared to the direction of the β-strands, the direction of the helical segments is generally anti-parallel to the β-strands (Fig. 5). | |||
In some Rossmann fold domains, the segments in between the β-strands may include a complex series of helical and coiled segments (for example see [[3bhi]]). | |||
==Evolutionary origin of the βαβ fold == | ==Evolutionary origin of the βαβ fold == | ||