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-Structure paper
Title | Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM. |
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Journal, issue, pages | Acta Crystallogr. D Biol. Crystallogr., Vol. 64, Page 178-188, Year 2008 |
Publish date | May 18, 2007 (structure data deposition date) |
Authors | Alahuhta, M. / Casteleijn, M.G. / Neubauer, P. / Wierenga, R.K. |
External links | Acta Crystallogr. D Biol. Crystallogr. / PubMed:18219118 |
Methods | X-ray diffraction |
Resolution | 1.18 - 2.3 Å |
Structure data | PDB-2v0t: PDB-2v2c: PDB-2v2d: PDB-2v2h: |
Chemicals | ChemComp-SO4: ChemComp-EPE: ChemComp-HOH: ChemComp-PGA: ChemComp-PO4: ChemComp-CL: |
Source |
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Keywords | ISOMERASE / SOMERASE / TIM-BARREL / GLYCOSOME / GLYCOLYSIS / ENGINEERING / PENTOSE SHUNT / POINT MUTATION / TIM / 2PG / A178L / LOOP6 / HINGE / LOOP-6 / ENZYME / FATTY ACID BIOSYNTHESIS / TRIOSEPHOSPHATE ISOMERASE / GLUCONEOGENESIS / LIPID SYNTHESIS / 2-PHOSPHO GLYCOLLATE / MONOMERIC / 2-PHOSPHO GLYCOLATE |