1mpm | pdb_00001mpm

MALTOPORIN MALTOSE COMPLEX

spinqualitylabelsall models 1mpm, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mpm is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: BGC, GLC, MG, PRD_900018 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LAMB_ECOLI Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ("greasy slide") of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda.[HAMAP-Rule:MF_01301] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed BACKGROUND: 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. RESULTS: The crystal structures of maltoporin in complex with maltose, maltotriose and maltohexaose reveal an extended binding site within the maltoporin channel. The maltooligosaccharides are in apolar van der Waals contact with the 'greasy slide', a hydrophobic path that is composed of aromatic residues and located at the channel lining. At the constriction of the channel the sugars are tightly surrounded by protein side chains and form an extensive hydrogen-bonding network with ionizable amino-acid residues. CONCLUSION: Hydrophobic interactions with the greasy slide guide the sugar into and through the channel constriction. The glucosyl-binding subsites at the channel constriction confer stereospecificity to the channel along with the ability to scavenge substrate at low concentrations. Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway.,Dutzler R, Wang YF, Rizkallah P, Rosenbusch JP, Schirmer T Structure. 1996 Feb 15;4(2):127-34. PMID:8805519 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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