The　maltose　transporter　from　Escherichia　coli　is　one　of　the　ATP-binding　cassette　(ABC)　transporters　that　utilize　the　energy　from　ATP　hydrolysis　to　translocate　substrates　across　cellular　membranes.　Until　2011,　three　crystal　structures　have　been　determined　for　maltose　transporter　at　different　states　in　the　process　of　transportation.　Here,　based　on　these　crystal　structures,　the　allosteric　pathway　from　the　resting　state　(inward-facing)　to　the　catalytic　intermediate　state　(outward-facing)　is　studied　by　applying　an　adaptive　anisotropic　network　model.　The　results　suggest　that　the　allosteric　transitions　proceed　in　a　coupled　way.　The　closing　of　the　nucleotide-binding　domains　occurs　first,　and　subsequently　this　conformational　change　is　propagated　to　the　transmembrane　domains　(TMD)　via　the　EAA　and　EAS　loops,　and　then　to　the　maltose-binding　protein,　which　facilitates　the　translocation　of　the　maltose.　It　is　also　found　that　there　exist　nonrigid-body　and　asymmetric　movements　in　the　TMD.　The　cytoplasmic　gate　may　only　play　the　role　of　allosteric　propagation　during　the　transition　from　the　pretranslocation　to　outward-facing　states.　In　addition,　the　results　show　that　the　movment　of　the　helical　subdomain　towards　the　RecA-like　subdomain　mainly　occurs　in　the　earlier　stages　of　the　transition.　These　results　can　provide　some　insights　into　the　understanding　of　the　mechanism　of　ABC　transporters.　(c)　2013　Wiley　Periodicals,　Inc.　Biopolymers　101:　758-768,　2014.