Banks R D, Blake C C, Evans P R, Haser R, Rice D W, Hardy G W, Merrett M, Phillips A W
Nature. 1979 Jun 28;279(5716):773-7. doi: 10.1038/279773a0.
The fitting of sequenced peptides to a high-resolution X-ray map of phosphoglycerate kinase has yielded the complete sequence and structure of the horse muscle enzyme. Metal ADP and ATP substrates are bound to one of the two widely separated domains in an environment that seems unsuitable for phosphoglycerate binding. The most plausible binding site for the phosphoglycerate substrate is on the other domain about 10 A from the ATP, which implies the possibility of a large scale hinge-bending of the domains to bring the two substrates together in a water-free environment for catalysis.
将测序得到的肽段与磷酸甘油酸激酶的高分辨率X射线图谱进行拟合，得到了马肌肉中该酶的完整序列和结构。金属ADP和ATP底物结合在两个相距甚远的结构域之一中，所处环境似乎不适合磷酸甘油酸结合。磷酸甘油酸底物最可能的结合位点在另一个结构域上，距离ATP约10埃，这意味着两个结构域可能会发生大规模的铰链弯曲，以便在无水环境中将两种底物聚集在一起进行催化。
