Phillips G N, Arduini R M, Springer B A, Sligar S G
Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251.
Proteins. 1990;7(4):358-65. doi: 10.1002/prot.340070407.
Crystals have been grown of myoglobin produced in Escherichia coli from a synthetic gene, and the structure has been solved to 1.9 A resolution. The space group of the crystals is P6, which is different from previously solved myoglobin crystal forms. The synthetic myoglobin is essentially identical to myoglobin isolated from sperm whale tissue, except for the retention of the initiator methionine at the N-terminus and the substitution of asparagine for aspartic acid at position 122. Superposition of the coordinates of native and synthetic sperm whale myoglobins reveals only minor changes in the positions of main chain atoms and reorientation of some surface side chains. Crystals of variants of the "synthetic" myoglobin have also been grown for structural analysis of the role of key amino acid residues in ligand binding and specificity.
已通过合成基因在大肠杆菌中生产出肌红蛋白晶体，其结构已解析至1.9埃分辨率。晶体的空间群为P6，这与先前解析的肌红蛋白晶体形式不同。合成肌红蛋白与从抹香鲸组织中分离出的肌红蛋白基本相同，只是在N端保留了起始甲硫氨酸，并且在第122位天冬氨酸被天冬酰胺取代。天然和合成抹香鲸肌红蛋白坐标的叠加显示，主链原子位置仅有微小变化，一些表面侧链重新定向。还培养了“合成”肌红蛋白变体的晶体，用于对关键氨基酸残基在配体结合和特异性中的作用进行结构分析。
