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41.
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The structure of the tightly bound complex of the globular myosin head with F-actin is the key to understanding important details of the mechanism of how the actin-myosin motor functions. The current notion on this complex is based on the docking of known atomic structures of constituent proteins into low-resolution electron-density maps. The atomic structure of the complex was refined by the molecular mechanics method, which consists in minimizing the energy of molecular interaction and which makes it possible to optimize not only the relative position of protein backbones as rigid bodies, but also the position of side chains on the protein interface. The structure calculated using ICM-Pro software, on the one hand, is close to the model obtained using electron microscopy; on the other hand, it ensures the best calculated interaction energy and accounts for the results of mutagenesis experiments. On the basis of the structure obtained, we can suggest the molecular mechanisms underlying the actin-activated release of ATP hydrolysis products from myosin and the decrease in the affinity of myosin for actin upon binding of nucleotides. 相似文献
43.
cDNA sequence and predicted primary structure of the gamma subunit from the ATP synthase from Chlamydomonas reinhardtii 总被引:3,自引:0,他引:3
The 1701-base nucleotide sequence (not including the poly(A) tail) of a cDNA for the gamma subunit of the ATP synthase from Chlamydomonas reinhardtii was determined. A start translation sequence, 23 bases in from the 5' end, initiates an 1074-base-long open reading frame. The sequence of the first 21 amino acids at the amino-terminal end of the mature gamma subunit from C. reinhardtii was determined and compared to the deduced amino acid sequence of the open reading frame. From this it was determined that the mature protein contains 323 amino acids, with the first 35 amino acids probably being part of the transit peptide. The length of the mature protein is the same as that for the mature gamma subunit from spinach, for which only a few of the amino acids of the transit peptide are known. The similarity of the two mature proteins at the nucleotide level is 56% while at the amino acid level it is 77%. In addition, the 3 cysteines, which in spinach are involved in the energy-linked catalytic functions of the ATP synthase, are conserved in the predicted amino acid sequence for the gamma subunit from C. reinhardtii. In contrast, the mature C. reinhardtii gamma subunit contains 3 additional cysteine residues not found in the spinach gamma subunit. 相似文献
44.
Wei Lu 《Evolution; international journal of organic evolution》2020,74(8):1879-1880
What determines the rate at which species adapt to new climatic conditions? Weaver et al. found that the evolution of short larval periods promotes climatic niche evolution in salamanders in the genus Desmognathus. 相似文献
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A. Yu. Kudeyarova 《Biology Bulletin》2006,33(3):293-303
The applicability of the nucleophilicity/electrophilicity concept to the explanation of mechanisms of formation and transformation of humic substances was considered. Sequential time changes in the structure and properties of humic substances in phosphatic soil have been revealed. Different elemental composition of humic and fulvic acids at different stages of humus transformation was due to different patterns of electron density distribution in phosphorus-modified fragments of humic molecules. The important role of metals and phosphorus in realization of different pathways of humic substance transformation was demonstrated. 相似文献
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Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module
Huaidong Zhang Guimin Zhang Chaoxiang Yao Muhammad Junaid Zhenghui Lu Houjin Zhang Yanhe Ma 《PloS one》2015,10(11)
Cellulases are the key enzymes used in the biofuel industry. A typical cellulase contains a catalytic domain connected to a carbohydrate-binding module (CBM) through a flexible linker. Here we report the structure of an atypical trimodular cellulase which harbors a catalytic domain, a CBM46 domain and a rigid CBM_X domain between them. The catalytic domain shows the features of GH5 family, while the CBM46 domain has a sandwich-like structure. The catalytic domain and the CBM46 domain form an extended substrate binding cleft, within which several tryptophan residues are well exposed. Mutagenesis assays indicate that these residues are essential for the enzymatic activities. Gel affinity electrophoresis shows that these tryptophan residues are involved in the polysaccharide substrate binding. Also, electrostatic potential analysis indicates that almost the entire solvent accessible surface of CelB is negatively charged, which is consistent with the halophilic nature of this enzyme. 相似文献
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