Ramachandran outlier
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However, sometimes Ramachandran outliers might play a special role in function. See for example the case of Ser-200 in the structure <scene name='76/762493/1ea5_color_sec_struct/3'>1ea5</scene>. Let's draw its <jmol><jmolLink><script>calculate structure;select protein;cartoon only;color structure;plot ramachandran</script><text>Ramachandran Plot</text></jmolLink></jmol>. | However, sometimes Ramachandran outliers might play a special role in function. See for example the case of Ser-200 in the structure <scene name='76/762493/1ea5_color_sec_struct/3'>1ea5</scene>. Let's draw its <jmol><jmolLink><script>calculate structure;select protein;cartoon only;color structure;plot ramachandran</script><text>Ramachandran Plot</text></jmolLink></jmol>. | ||
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| + | ''The following green links require that you '''first''' click the above green link to Ramachandran Plot.'' | ||
Notice that the residues in <jmol><jmolLink><script>display sheet</script><text>beta sheets</text></jmolLink></jmol> are colored in yellow, the residues in <jmol><jmolLink><script>display helix</script><text>alpha helix</text></jmolLink></jmol> colored in magenta, <jmol><jmolLink><script>display turn</script><text>beta turn</text></jmolLink></jmol> in blue and <jmol><jmolLink><script>display all; hide sheet,helix,turn;</script><text>others</text></jmolLink></jmol> in white. At any time you may <jmol><jmolLink><script>display all</script><text>display all</text></jmolLink></jmol> residues. | Notice that the residues in <jmol><jmolLink><script>display sheet</script><text>beta sheets</text></jmolLink></jmol> are colored in yellow, the residues in <jmol><jmolLink><script>display helix</script><text>alpha helix</text></jmolLink></jmol> colored in magenta, <jmol><jmolLink><script>display turn</script><text>beta turn</text></jmolLink></jmol> in blue and <jmol><jmolLink><script>display all; hide sheet,helix,turn;</script><text>others</text></jmolLink></jmol> in white. At any time you may <jmol><jmolLink><script>display all</script><text>display all</text></jmolLink></jmol> residues. | ||
| - | Only Gly are allowed in the lower right quarter. If we <jmol><jmolLink><script>display all; hide Gly</script><text>hide Gly</text></jmolLink></jmol> from the plot, will find the <jmol><jmolLink><script>select [SER]200:A;color selectionHalos green;selectionHalos on;label "\u03C6 =\u20%5.1[phi]\uB0|\u03C8 =\u20%5.1[psi]\uB0";set labelOffset 10 0;</script><text>Ser 200</text></jmolLink></jmol>, with phi/psi angles considered non-favourable for Serine. | + | Only Gly are allowed in the lower right quarter. If we <jmol><jmolLink><script>display all; hide Gly</script><text>hide Gly</text></jmolLink></jmol> from the plot, we will find the <jmol><jmolLink><script>select [SER]200:A;color selectionHalos green;selectionHalos on;label "\u03C6 =\u20%5.1[phi]\uB0|\u03C8 =\u20%5.1[psi]\uB0";set labelOffset 10 0;</script><text>Ser 200</text></jmolLink></jmol>, with phi/psi angles considered non-favourable for Serine. |
However, in this case, a Ramachandran-misplaced residue (Ser 200) seems to play an important role in the function of this structure, a member of the alpha/beta hydrolase fold <ref>pmid 1409539</ref>. | However, in this case, a Ramachandran-misplaced residue (Ser 200) seems to play an important role in the function of this structure, a member of the alpha/beta hydrolase fold <ref>pmid 1409539</ref>. | ||
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</StructureSection> | </StructureSection> | ||
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== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Ramachandran outlier
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References
- ↑ RAMACHANDRAN GN, RAMAKRISHNAN C, SASISEKHARAN V. Stereochemistry of polypeptide chain configurations. J Mol Biol. 1963 Jul;7:95-9. PMID:13990617
- ↑ Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, et al.. The alpha/beta hydrolase fold. Protein Eng. 1992 Apr;5(3):197-211. PMID:1409539
