1gfp
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1gfp.gif|left|200px]] | [[Image:1gfp.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1gfp", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1gfp| PDB=1gfp | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''OMPF PORIN (MUTANT R42C)''' | '''OMPF PORIN (MUTANT R42C)''' | ||
| Line 27: | Line 24: | ||
[[Category: Lou, K L.]] | [[Category: Lou, K L.]] | ||
[[Category: Schirmer, T.]] | [[Category: Schirmer, T.]] | ||
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | [[Category: | + | [[Category: Outer membrane]] |
| - | [[Category: | + | [[Category: Porin]] |
| - | [[Category: | + | [[Category: Transmembrane protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:30:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:30, 2 May 2008
OMPF PORIN (MUTANT R42C)
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
1GFP 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 Page seeded by OCA on Fri May 2 17:30:25 2008
