2f1c
From Proteopedia
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| - | [[Image:2f1c.gif|left|200px]] | + | [[Image:2f1c.gif|left|200px]] |
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| - | '''Crystal structure of the monomeric porin OmpG''' | + | {{Structure |
| + | |PDB= 2f1c |SIZE=350|CAPTION= <scene name='initialview01'>2f1c</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= ompG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the monomeric porin OmpG''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F1C is a [ | + | 2F1C 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=2F1C OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the monomeric porin OmpG., Subbarao GV, van den Berg B, J Mol Biol. 2006 Jul 21;360(4):750-9. Epub 2006 Jun 2. PMID:[http:// | + | Crystal structure of the monomeric porin OmpG., Subbarao GV, van den Berg B, J Mol Biol. 2006 Jul 21;360(4):750-9. Epub 2006 Jun 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16797588 16797588] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta barrel]] | [[Category: beta barrel]] | ||
| - | ''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 16:46:52 2008'' |
Revision as of 14:46, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | |||||||
| Gene: | ompG (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the monomeric porin OmpG
Overview
The outer membrane (OM) of Gram-negative bacteria contains a large number of channel proteins that mediate the uptake of ions and nutrients necessary for growth and functioning of the cell. An important group of OM channel proteins are the porins, which mediate the non-specific, diffusion-based passage of small (<600 Da) polar molecules. All porins of Gram-negative bacteria that have been crystallized to date form stable trimers, with each monomer composed of a 16-stranded beta-barrel with a relatively narrow central pore. In contrast, the OmpG porin is unique, as it appears to function as a monomer. We have determined the X-ray crystal structure of OmpG from Escherichia coli to a resolution of 2.3 A. The structure shows a 14-stranded beta-barrel with a relatively simple architecture. Due to the absence of loops that fold back into the channel, OmpG has a large ( approximately 13 A) central pore that is considerably wider than those of other E. coli porins, and very similar in size to that of the toxin alpha-hemolysin. The architecture of the channel, together with previous biochemical and other data, suggests that OmpG may form a non-specific channel for the transport of larger oligosaccharides. The structure of OmpG provides the starting point for engineering studies aiming to generate selective channels and for the development of biosensors.
About this Structure
2F1C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the monomeric porin OmpG., Subbarao GV, van den Berg B, J Mol Biol. 2006 Jul 21;360(4):750-9. Epub 2006 Jun 2. PMID:16797588
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