1MPO
MALTOPORIN MALTOHEXAOSE COMPLEX
Summary for 1MPO
Entry DOI | 10.2210/pdb1mpo/pdb |
Related PRD ID | PRD_900030 |
Descriptor | MALTOPORIN, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | membrane protein, specific porin, beta barrel membrane protein, sugar transport, beta barrel |
Biological source | Escherichia coli |
Cellular location | Cell outer membrane ; Multi-pass membrane protein : P02943 |
Total number of polymer chains | 3 |
Total formula weight | 144836.43 |
Authors | Dutzler, R.,Schirmer, T. (deposition date: 1996-01-11, release date: 1997-03-12, Last modification date: 2024-11-20) |
Primary citation | Dutzler, R.,Wang, Y.F.,Rizkallah, P.J.,Rosenbusch, J.P.,Schirmer, T. Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure, 4:127-134, 1996 Cited by PubMed Abstract: Maltoporin (which is encoded by the lamB gene) facilitates the translocation of maltodextrins across the outer membrane of E. coli. In particular, it is indispensable for the transport of long maltooligosaccharides, as these do not pass through non-specific porins. An understanding of this intriguing capability requires elucidation of the structural basis. PubMed: 8805519DOI: 10.1016/S0969-2126(96)00016-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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