1gfn

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[[Image:1gfn.jpg|left|200px]]
 
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{{Structure
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==OMPF PORIN DELETION (MUTANT DELTA 109-114)==
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|PDB= 1gfn |SIZE=350|CAPTION= <scene name='initialview01'>1gfn</scene>, resolution 3.1&Aring;
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<StructureSection load='1gfn' size='340' side='right'caption='[[1gfn]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>
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<table><tr><td colspan='2'>[[1gfn]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GFN FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gfn OCA], [https://pdbe.org/1gfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gfn RCSB], [https://www.ebi.ac.uk/pdbsum/1gfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gfn ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gfn OCA], [http://www.ebi.ac.uk/pdbsum/1gfn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gfn RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/OMPF_ECOLI OMPF_ECOLI] Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.<ref>PMID:19721064</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/1gfn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gfn ConSurf].
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<div style="clear:both"></div>
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'''OMPF PORIN DELETION (MUTANT DELTA 109-114)'''
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==See Also==
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*[[Porin 3D structures|Porin 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lou, K L.]]
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[[Category: Lou K-L]]
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[[Category: Schirmer, T.]]
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[[Category: Schirmer T]]
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[[Category: membrane protein]]
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[[Category: outer membrane]]
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[[Category: porin]]
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[[Category: transmembrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:43:01 2008''
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Current revision

OMPF PORIN DELETION (MUTANT DELTA 109-114)

PDB ID 1gfn

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