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Sandbox GGC7

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== Triose phosphate isomerase ==
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==Name of your molecule==
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<StructureSection load='5CSR' size='340' side='right' caption='Triose phosphate isomerase' scene='75/752270/Intro/2>
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<StructureSection load='5CSR' size='340' side='right' caption='Triose phosphate isomerase' scene=''>
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Triosephosphate isomerase (TPI or TIM) is a functionally and structurally well-known enzyme that play a crucial role in glycolytic and gluconeogenic metabolism. TPI interconverts dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P) <ref>DOI:10.1371/journal.pone.0145331</ref>
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This is a default text for your page '''Sandbox GGC7'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Structure and Function ==
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== Function ==
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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.
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== Disease ==
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== Relevance ==
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== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
== References ==
== References ==
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<references/><scene name='75/752270/Tatpi/4'></scene>
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<references/>

Revision as of 19:06, 23 February 2018

Name of your molecule

Triose phosphate isomerase

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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