1gfn
From Proteopedia
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| - | [[Image:1gfn.jpg|left|200px]] | + | [[Image:1gfn.jpg|left|200px]] |
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| - | '''OMPF PORIN DELETION (MUTANT DELTA 109-114)''' | + | {{Structure |
| + | |PDB= 1gfn |SIZE=350|CAPTION= <scene name='initialview01'>1gfn</scene>, resolution 3.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''OMPF PORIN DELETION (MUTANT DELTA 109-114)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GFN is a [ | + | 1GFN 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=1GFN OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis., Lou KL, Saint N, Prilipov A, Rummel G, Benson SA, Rosenbusch JP, Schirmer T, J Biol Chem. 1996 Aug 23;271(34):20669-75. PMID:[http:// | + | Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis., Lou KL, Saint N, Prilipov A, Rummel G, Benson SA, Rosenbusch JP, Schirmer T, J Biol Chem. 1996 Aug 23;271(34):20669-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8702816 8702816] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transmembrane protein]] | [[Category: transmembrane protein]] | ||
| - | ''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 11:22:24 2008'' |
Revision as of 09:22, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
OMPF PORIN DELETION (MUTANT DELTA 109-114)
Overview
OmpF porin is a nonspecific pore protein from the outer membrane of Escherichia coli. Previously, a set of mutants was selected that allow the passage of long maltodextrins that do not translocate through the wild-type pore. Here, we describe the crystal structures of four point mutants and one deletion mutant from this set; their functional characterization is reported in the accompanying paper (Saint, N., Lou, K.-L., Widmer, C., Luckey, M., Schirmer, T., Rosenbusch, J. P. (1996) J. Biol. Chem. 271, 20676-20680). All mutations have a local effect on the structure of the pore constriction and result in a larger pore cross-section. Substitution of each of the three closely packed arginine residues at the pore constriction (Arg-42, Arg-82, and Arg-132) by shorter uncharged residues causes rearrangement of the adjacent basic residues. This demonstrates mutual stabilization of these residues in the wild-type porin. Deletion of six residues from the internal loop (Delta109-114) results in disorder of seven adjacent residues but does not alter the structure of the beta-barrel framework. Thus, the large hollow beta-barrel motif can be regarded as an autonomous structure.
About this Structure
1GFN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis., Lou KL, Saint N, Prilipov A, Rummel G, Benson SA, Rosenbusch JP, Schirmer T, J Biol Chem. 1996 Aug 23;271(34):20669-75. PMID:8702816
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