1hxx: Difference between revisions

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New page: left|200px<br /><applet load="1hxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hxx, resolution 2.2Å" /> '''OMPF PORIN MUTANT Y10...
 
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[[Image:1hxx.gif|left|200px]]<br /><applet load="1hxx" size="450" color="white" frame="true" align="right" spinBox="true"
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'''OMPF PORIN MUTANT Y106F'''<br />


==Overview==
==OMPF PORIN MUTANT Y106F==
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.
<StructureSection load='1hxx' size='340' side='right'caption='[[1hxx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==About this Structure==
==See Also==
1HXX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with C8E as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HXX OCA].
*[[Porin 3D structures|Porin 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11371193 11371193]
__TOC__
</StructureSection>
[[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: C8E]]
[[Category: beta barrel]]
[[Category: membrane protein]]
[[Category: porin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:53:56 2007''

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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