a Istituto di Biochimica e Biochimica Clinica , Università Cattolica del Sacro Cuore , L.go F. Vito 1, Rome 00168 , Italy.
b Molecular Microbiology and Structural Biochemistry Institute , UMR5086 CNRS Univ-Lyon , Cedex 7, Lyon F-69367 , France.
J Biomol Struct Dyn. 2018 Nov;36(14):3666-3679. doi: 10.1080/07391102.2017.1395767. Epub 2017 Nov 7.
The unique eukaryotic-like Ser/Thr protein kinases of Streptococcus pneumoniae, StkP, plays a primary role in the cell division process. It is composed of an intracellular kinase domain, a transmembrane helix and four extracellular PASTA subunits. PASTA domains were shown to interact with cell wall fragments but the key questions related to the molecular mechanism governing ligand recognition remain unclear. To address this issue, the full-length structural model of StkP was generated by combining small-angle X-ray scattering data with the results of computer simulations. Docking and molecular dynamics studies on the generated three-dimensional model structure reveal the possibility of peptidoglycan fragment binding at the hinge regions between PASTA subunits with a preference for a bent hinge between PASTA3 and PASTA4.
肺炎链球菌中独特的真核样丝氨酸/苏氨酸蛋白激酶 StkP 在细胞分裂过程中发挥主要作用。它由一个细胞内激酶结构域、一个跨膜螺旋和四个细胞外 PASTA 亚基组成。已经表明 PASTA 结构域与细胞壁片段相互作用，但与配体识别相关的关键问题仍不清楚。为了解决这个问题，通过将小角度 X 射线散射数据与计算机模拟结果相结合，生成了 StkP 的全长结构模型。对生成的三维模型结构进行对接和分子动力学研究表明，肽聚糖片段有可能在 PASTA 亚基之间的铰链区域结合，并且 PASTA3 和 PASTA4 之间的弯曲铰链具有优先性。
