The structures of BtuCD and MscS and their implications for transporter and channel function |
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Authors: | Bass Randal B Locher Kaspar P Borths Elizabeth Poon Yan Strop Pavel Lee Allen Rees Douglas C |
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Affiliation: | Division of Chemistry and Chemical Engineering, 114-96, California Institute of Technology, Pasadena, CA 91125, USA. |
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Abstract: | The passage of most molecules across biological membranes is mediated by specialized integral membrane proteins known as channels and transporters. Although these transport families encompass a wide range of functions, molecular architectures and mechanisms, there are common elements that must be incorporated within their structures, namely the translocation pathway, ligand specificity elements and regulatory sensors to control the rate of ligand flow across the membrane. This minireview discusses aspects of the structure and mechanism of two bacterial transport systems, the stretch-activated mechanosensitive channel of small conductance (MscS) and the ATP-dependent vitamin B12 uptake system (BtuCD), emphasizing their general implications for transporter function. |
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Keywords: | Transport protein Mechanosensitive channel ATP binding cassette transporter Membrane protein structure |
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