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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of triosephosphate isomerase (TIM) from Methanocaldococcus jannaschii
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Structure of triosephosphate isomerase (TIM) from Methanocaldococcus jannaschii

机译：triosephosphate结构异构酶(TIM)

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摘要

The crystal structure of a recombinant triosephosphate isomerase (TIM) from the archaeabacterium Methanocaldococcus jannaschii has been determined at a resolution of 2.3 angstrom using X-ray diffraction data from a tetartohedrally twinned crystal. M. jannaschii TIM (MjTIM) is tetrameric, as suggested by solution studies and from the crystal structure, as is the case for two other structurally characterized archaeal TIMs. The archaeabacterial TIMs are shorter compared with the dimeric TIMs; the insertions in the dimeric TIMs occur in the vicinity of the tetramer interface, resulting in a hindrance to tetramerization in the dimeric TIMs. The charge distribution on the surface of the archaeal TIMs also facilitates tetramerization. Analysis of the barrel interactions in TIMs suggests that these interactions are unlikely to account for the thermal stability of the archaeal TIMs. A novelty of the unliganded structure of MjTIM is the complete absence of electron density for the loop 6 residues. The disorder of this loop could be ascribed to a missing salt bridge between residues at the N- and C-terminal ends of the loop in MjTIM.
机译：的晶体结构重组triosephosphate异构酶(TIM)已经确定在分辨率为2.3使用x射线衍射数据从埃tetartohedrally成双成对的晶体。蒂姆•(MjTIM)是四聚物的建议解决方案的研究和晶体结构,作为两个结构的情况古细菌蒂姆斯特点。蒂姆斯短比二聚的蒂姆斯;插入的二聚的蒂姆斯出现在四聚物界面附近,导致一个阻碍tetramerization二聚的蒂姆。古细菌蒂姆也便利tetramerization。相互作用与蒂姆斯表明,这些相互作用是不太可能的古细菌蒂姆的热稳定性。unliganded MjTIM结构的完全没有电子密度的循环6残留。归因于缺少盐之间的桥梁残留在N - c端结束的在MjTIM循环。

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