The　Glutamine-Binding　Protein　(GlnBP)　of　Escherichia　coil　is　responsible　for　the　first　step　in　the　active　transport　of　glutamine　across　the　cytoplasmic　membrane.　In　present　work,　we　explored　the　allosteric　pathway　of　GInBP　from　the　open　to　closed　states　during　the　substrate　binding　process　with　the　adaptive　anisotropic　network　model　(aANM).　The　results　show　that　the　allosteric　transition　proceeds　in　a　coupled　way　and　is　more　likely　to　be　driven　by　the　movement　of　hinge　regions.　The　large-scale　hinge-bending　motion　between　the　large　and　small　domains　occurs,　accompanied　by　an　interdomain　twisting　motion　which　proceeds　mainly　in　the　middle　stage.　The　cooperative　motion　between　the　dominant　hinge-bending　motion　and　the　twisting　motion　exerts　a　crucial　role　in　the　open-closed　motion　of　GlnBP.　These　results　are　in　close　agreement　with　previous　experimental　and　theoretical　data,　implying　that　the　topology　structure　plays　a　crucial　role　in　the　allosteric　transition　process　of　GInBP.　(C)　2017　Elsevier　B.V.　All　rights　reserved.