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| [[Image:2r6g.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2r6g| PDB=2r6g | SCENE= }} | | {{STRUCTURE_2r6g| PDB=2r6g | SCENE= }} |
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| '''The Crystal Structure of the E. coli Maltose Transporter'''
| | ===The Crystal Structure of the E. coli Maltose Transporter=== |
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| ==Overview==
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| The maltose uptake system of Escherichia coli is a well-characterized member of the ATP-binding cassette transporter superfamily. Here we present the 2.8-A crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP. This structure, stabilized by a mutation that prevents ATP hydrolysis, captures the ATP-binding cassette dimer in a closed, ATP-bound conformation. Maltose is occluded within a solvent-filled cavity at the interface of the two transmembrane subunits, about halfway into the lipid bilayer. The binding protein docks onto the entrance of the cavity in an open conformation and serves as a cap to ensure unidirectional translocation of the sugar molecule. These results provide direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP. | | The line below this paragraph, {{ABSTRACT_PUBMED_18033289}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18033289 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18033289}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Sugar transport]] | | [[Category: Sugar transport]] |
| [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:19:32 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:34:28 2008'' |