Rossmann fold: Difference between revisions

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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.


<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' />
<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' />


<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>




==Extension of the beta sheet by additional strands==
==Extension of the beta sheet by additional strands==
[[Image:3-phosphoglycerate_dehydrogenase-2P9E-sheet.png|250px|left|thumb| Fig. 4. 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.]]
[[Image:3-phosphoglycerate_dehydrogenase-2P9E-sheet.png|400px|right|thumb| Fig. 4. 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 &beta;&alpha;&beta; fold, the &beta;-strands may be part of a larger &beta;-sheet with up to seven &beta;-strands. Figure 4 shows five strands forming a &beta;-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 &alpha;-helix segments.
In many (but not all) proteins with &beta;&alpha;&beta; fold, the &beta;-strands may be part of a larger &beta;-sheet with up to seven &beta;-strands. Figure 4 shows five strands forming a &beta;-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 &alpha;-helix segments.


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Israel Hanukoglu, Angel Herraez, Karsten Theis