Biesecker G, Harris J I, Thierry J C, Walker J E, Wonacott A J
Nature. 1977 Mar 24;266(5600):328-33. doi: 10.1038/266328a0.
The glyceraldehyde 3-phosphate dehydogenase holoenzyme of Bacillus stearothermophilus possesses precise 222 symmetry: in this respect it differs from the reported structure of the lobster muscle enzyme. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects. Three additional salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer.
嗜热脂肪芽孢杆菌的甘油醛-3-磷酸脱氢酶全酶具有精确的222对称性：在这方面它不同于已报道的龙虾肌肉酶的结构。活性位点对通过一个柔性多肽环相连，该环可能介导导致协同效应的结构变化。每个亚基与其他亚基形成的另外三个盐桥将对四聚体的热稳定性起主要作用。
