1gfp: Difference between revisions

Revision as of 05:12, 1 July 2008

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File:1gfp.png

Template:STRUCTURE 1gfp

OMPF PORIN (MUTANT R42C)OMPF PORIN (MUTANT R42C)

Template:ABSTRACT PUBMED 8702816

About this StructureAbout this Structure

1GFP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''OMPF PORIN (MUTANT R42C)'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8702816}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8702816 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8702816}}
 ==About this Structure==
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 [[Category: Porin]]
 [[Category: Transmembrane protein]]
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