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Sandbox GGC7
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== Structure and Function == | == Structure and Function == | ||
| - | 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_site_g3p/1'>active site</scene> includes conserved residues: Glu 137, His 89, Lys 9. The catalytic base is Gly 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 Gly143, Gly 175, Ala 196 and Ser 197 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_site_g3p/1'>active site</scene> includes conserved residues: <scene name='75/752270/Gly137/2'>Glu 137, His 89, Lys 9</scene>. The catalytic base is Gly 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 Gly143, Gly 175, Ala 196 and Ser 197 residues. |
Revision as of 01:47, 1 May 2017
Triose phosphate isomerase
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References
- ↑ Park SH, Kim HS, Park MS, Moon S, Song MK, Park HS, Hahn H, Kim SJ, Bae E, Kim HJ, Han BW. Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum. PLoS One. 2015 Dec 28;10(12):e0145331. doi: 10.1371/journal.pone.0145331., eCollection 2015. PMID:26709515 doi:http://dx.doi.org/10.1371/journal.pone.0145331
