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Sandbox GGC7
From Proteopedia
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This crystal structure of trioseohosphate isomerase was isolated from Thermoplasma acidophilum, an archaeal species, and therefore was called TaTPI. <scene name='75/752270/Tatpi/2'>TaTPI</scene> contain four copies of TaTPI monomer in the asymmetric unit, comprising <scene name='75/752270/Tatpi_homodimer/1'>two homodimers</scene>. TaTPI is composed of 216 amino acid residues, which is shorter compare to other TPIs from bacterial and eukaryotic species. Each subunit forms a <scene name='75/752270/Tim_barrel/1'>TIM barrel</scene> in which 8α helices (in pink) alternate with 8β sheets (in yellow) to form backbone of the protein. Hydrophobic chains form the core enzyme whereas hydrophilic found near the ends of the barrel where exposed to solvent. Each subunit has it own active site and only active as a dimer. The <scene name='75/752270/Active_glu137_his89_lys9/1'>active site</scene> includes conserved residues: <scene name='75/752270/Gly137/2'>Glu 137, His 89, Lys 9</scene>. The catalytic base is Glu 137. The oxyanion hole is formed between nitrogen of Lys 9 and of His 89 with O2 of G3P. The phosphate group of G3P forms hydrogen bonds with backbone nitrogen atoms of <scene name='75/752270/Active_glu137_his89_lys9/2'>Gly143, Gly 175, Ala 196 and Ser 197</scene> residues. | This crystal structure of trioseohosphate isomerase was isolated from Thermoplasma acidophilum, an archaeal species, and therefore was called TaTPI. <scene name='75/752270/Tatpi/2'>TaTPI</scene> contain four copies of TaTPI monomer in the asymmetric unit, comprising <scene name='75/752270/Tatpi_homodimer/1'>two homodimers</scene>. TaTPI is composed of 216 amino acid residues, which is shorter compare to other TPIs from bacterial and eukaryotic species. Each subunit forms a <scene name='75/752270/Tim_barrel/1'>TIM barrel</scene> in which 8α helices (in pink) alternate with 8β sheets (in yellow) to form backbone of the protein. Hydrophobic chains form the core enzyme whereas hydrophilic found near the ends of the barrel where exposed to solvent. Each subunit has it own active site and only active as a dimer. The <scene name='75/752270/Active_glu137_his89_lys9/1'>active site</scene> includes conserved residues: <scene name='75/752270/Gly137/2'>Glu 137, His 89, Lys 9</scene>. The catalytic base is Glu 137. The oxyanion hole is formed between nitrogen of Lys 9 and of His 89 with O2 of G3P. The phosphate group of G3P forms hydrogen bonds with backbone nitrogen atoms of <scene name='75/752270/Active_glu137_his89_lys9/2'>Gly143, Gly 175, Ala 196 and Ser 197</scene> residues. | ||
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| - | == Disease == | ||
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| - | == Relevance == | ||
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| - | == Structural highlights == | ||
| - | <scene name='75/752270/Tatpi/3'>TaTPI</scene> | ||
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| - | </StructureSection> | ||
== References == | == References == | ||
| - | <references/><scene name='75/752270/Tatpi/4'> | + | <references/><scene name='75/752270/Tatpi/4'></scene> |
Revision as of 02:19, 1 May 2017
Triose phosphate isomerase
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