1mpm
From Proteopedia
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| - | [[Image:1mpm.jpg|left|200px]] | + | [[Image:1mpm.jpg|left|200px]] |
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| - | '''MALTOPORIN MALTOSE COMPLEX''' | + | {{Structure |
| + | |PDB= 1mpm |SIZE=350|CAPTION= <scene name='initialview01'>1mpm</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''MALTOPORIN MALTOSE COMPLEX''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MPM is a [ | + | 1MPM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPM OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8805519 8805519] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sugar transport]] | [[Category: sugar transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:34 2008'' |
Revision as of 10:46, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MALTOPORIN MALTOSE COMPLEX
Overview
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.
About this Structure
1MPM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 12:46:34 2008
