Cramer Jacob Flyvholm, Nordberg Peter A, Hajdu Janos, Lejon Sara
Department of Cell and Molecular Biology, Uppsala University, Biomedical Centre, Uppsala, Sweden.
FEBS Lett. 2007 Jul 10;581(17):3178-82. doi: 10.1016/j.febslet.2007.06.003. Epub 2007 Jun 12.
The albumin-binding domain, or GA module, of the peptostreptococcal albumin-binding protein expressed in pathogenic strains of Finegoldia magna is believed to be responsible for the virulence and increased growth rate of these strains. Here we present the 1.4A crystal structure of this domain, and compare it with the crystal structure of the GA-albumin complex. An analysis of protein-protein interactions in the two crystals, and the presence of multimeric GA species in solution, indicate the GA module is "sticky", and is capable of forming contacts with a range of protein surfaces. This might lead to interactions with different host proteins.
在大芬戈尔德菌致病菌株中表达的消化链球菌白蛋白结合蛋白的白蛋白结合结构域或GA模块,被认为是这些菌株毒力和生长速率增加的原因。在此,我们展示了该结构域的1.4埃晶体结构,并将其与GA-白蛋白复合物的晶体结构进行比较。对两种晶体中蛋白质-蛋白质相互作用的分析以及溶液中多聚体GA物种的存在表明,GA模块具有“粘性”,能够与一系列蛋白质表面形成接触。这可能导致与不同宿主蛋白发生相互作用。