1hxx: Difference between revisions

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[[Image:1hxx.gif|left|200px]]


<!--
==OMPF PORIN MUTANT Y106F==
The line below this paragraph, containing "STRUCTURE_1hxx", creates the "Structure Box" on the page.
<StructureSection load='1hxx' size='340' side='right'caption='[[1hxx]], [[Resolution|resolution]] 2.20&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'>[[1hxx]] 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=1HXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HXX 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]] 2.2&#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_1hxx| PDB=1hxx |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxx OCA], [https://pdbe.org/1hxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hxx RCSB], [https://www.ebi.ac.uk/pdbsum/1hxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxx 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/hx/1hxx_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=1hxx ConSurf].
<div style="clear:both"></div>


'''OMPF PORIN MUTANT Y106F'''
==See Also==
 
*[[Porin 3D structures|Porin 3D structures]]
 
== References ==
==Overview==
<references/>
The channel constriction of OmpF porin, a pore protein in the bacterial outer membrane, is highly charged due to the presence of three arginines (R42, R82, and R132) and two acidic residues (D113 and E117). The influence of these charges on ion conductance, ion selectivity, and voltage gating has been studied with mutants D113N/E117Q, R42A/R82A/R132A/D113N/E117Q, and V18K/G131K, which were designed to remove or add protein charge at the channel constriction. The crystal structures revealed no or only local changes compared to wild-type OmpF, thus allowing a comparative study. The single-channel conductance of the isosteric D113N/E117Q variant was found to be 2-fold reduced, and that of the pentuple mutant was 70% of the wild-type value, despite a considerably larger pore cross section. Ion selectivity was drastically altered by the mutations with cation/anion permeability ratios ranging from 1 to 12. Ion flow through these and eight other mutants, which have been characterized previously, was simulated by Brownian dynamics based on the detailed crystal structures. The calculated ion selectivity and relative channel conductance values agree well with the experimental data. This demonstrates that ion translocation through porin is mainly governed by pore geometry and charge, the two factors that are properly represented in the simulations.
__TOC__
 
</StructureSection>
==About this Structure==
1HXX 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=1HXX OCA].
 
==Reference==
Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation., Phale PS, Philippsen A, Widmer C, Phale VP, Rosenbusch JP, Schirmer T, Biochemistry. 2001 May 29;40(21):6319-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371193 11371193]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Phale, P S.]]
[[Category: Phale PS]]
[[Category: Phale, V P.]]
[[Category: Phale VP]]
[[Category: Philippsen, A.]]
[[Category: Philippsen A]]
[[Category: Rosenbusch, J P.]]
[[Category: Rosenbusch JP]]
[[Category: Schirmer, T.]]
[[Category: Schirmer T]]
[[Category: Widmer, C.]]
[[Category: Widmer C]]
[[Category: Beta barrel]]
[[Category: Membrane protein]]
[[Category: Porin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:20:43 2008''

Latest revision as of 10:31, 7 February 2024

OMPF PORIN MUTANT Y106FOMPF PORIN MUTANT Y106F

Structural highlights

1hxx is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OMPF_ECOLI Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Duval V, Nicoloff H, Levy SB. Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli. Antimicrob Agents Chemother. 2009 Nov;53(11):4944-8. doi: 10.1128/AAC.00787-09., Epub 2009 Aug 31. PMID:19721064 doi:10.1128/AAC.00787-09

1hxx, resolution 2.20Å

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