This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1gfo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:25, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gfo.jpg|left|200px]]
 
-
<!--
+
==OMPF PORIN (MUTANT R132P)==
-
The line below this paragraph, containing "STRUCTURE_1gfo", creates the "Structure Box" on the page.
+
<StructureSection load='1gfo' size='340' side='right'caption='[[1gfo]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1gfo]] 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=1GFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GFO FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
-
-->
+
<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>
-
{{STRUCTURE_1gfo| PDB=1gfo | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gfo OCA], [https://pdbe.org/1gfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gfo RCSB], [https://www.ebi.ac.uk/pdbsum/1gfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gfo ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/1gfo_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1gfo ConSurf].
 +
<div style="clear:both"></div>
-
'''OMPF PORIN (MUTANT R132P)'''
+
==See Also==
-
 
+
*[[Porin 3D structures|Porin 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
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.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1GFO 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=1GFO 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:[http://www.ncbi.nlm.nih.gov/pubmed/8702816 8702816]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Lou, K L.]]
+
[[Category: Lou K-L]]
-
[[Category: Schirmer, T.]]
+
[[Category: Schirmer T]]
-
[[Category: Membrane protein]]
+
-
[[Category: Outer membrane]]
+
-
[[Category: Porin]]
+
-
[[Category: Transmembrane protein]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:30:26 2008''
+

Current revision

OMPF PORIN (MUTANT R132P)

PDB ID 1gfo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools