Ketosteroid Isomerase: Difference between revisions
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Undo revision 1241055 by Laura M. Haynes (Talk) |
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===Beta-Sheet=== | ===Beta-Sheet=== | ||
[[Image:beta-turn.png|thumb|right|250px]] | |||
Each monomer of KSI contains a <scene name='User:Laura_M._Haynes/Sandbox_1/Beta-sheet/1'>six-strand mixed beta-sheet</scene>. Strand 1 of the β-sheet is composed of residues Glu43 to Gly47. Strand 2 is contains residues Ala34 to Asp38 and runs antiparallel to strand 1. Leu63 to Val74 make up strand 3 which runs antiparallel to strand 4 (Glu77 to Tyr88). Residues Arg91 to Phe104 and Lys108 to Gly124 form strands 5 and 6 respectively. Strand 5 runs antiparallel to strand 4, while strand 6 runs antiparallel to strand 5 and parallel to strand 1.<ref name="Wu" /> Each β-sheet contains two β-bulges: <scene name='User:Laura_M._Haynes/Sandbox_1/Beta_bulge_1/1'>Thr68 to Glu70 </scene> and <scene name='User:Laura_M._Haynes/Sandbox_1/Beta_bulge_3/1'>Phe116 to Asn120</scene>. Both the β-bulges participate in dimer-dimer interactions, potentially leading to their stabilization. The juxtaposition of the two β-bulges on each side of the sheet with a central proline residue creates a substantial <scene name='User:Laura_M._Haynes/Sandbox_1/Kink/1'>kink</scene> in the β-sheet.<ref name="Wu" /> | Each monomer of KSI contains a <scene name='User:Laura_M._Haynes/Sandbox_1/Beta-sheet/1'>six-strand mixed beta-sheet</scene>. Strand 1 of the β-sheet is composed of residues Glu43 to Gly47. Strand 2 is contains residues Ala34 to Asp38 and runs antiparallel to strand 1. Leu63 to Val74 make up strand 3 which runs antiparallel to strand 4 (Glu77 to Tyr88). Residues Arg91 to Phe104 and Lys108 to Gly124 form strands 5 and 6 respectively. Strand 5 runs antiparallel to strand 4, while strand 6 runs antiparallel to strand 5 and parallel to strand 1.<ref name="Wu" /> Each β-sheet contains two β-bulges: <scene name='User:Laura_M._Haynes/Sandbox_1/Beta_bulge_1/1'>Thr68 to Glu70 </scene> and <scene name='User:Laura_M._Haynes/Sandbox_1/Beta_bulge_3/1'>Phe116 to Asn120</scene>. Both the β-bulges participate in dimer-dimer interactions, potentially leading to their stabilization. The juxtaposition of the two β-bulges on each side of the sheet with a central proline residue creates a substantial <scene name='User:Laura_M._Haynes/Sandbox_1/Kink/1'>kink</scene> in the β-sheet.<ref name="Wu" /> | ||
