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[[Image:2prn.jpg|left|200px]]
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{{STRUCTURE_2prn|  PDB=2prn  |  SCENE=  }}
'''RHODOPSEUDOMONAS BLASTICA PORIN, TRIPLE MUTANT E1M, E99W, A116W'''


==RHODOPSEUDOMONAS BLASTICA PORIN, TRIPLE MUTANT E1M, E99W, A116W==
<StructureSection load='2prn' size='340' side='right'caption='[[2prn]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2prn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fuscovulum_blasticum Fuscovulum blasticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PRN 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]] 1.93&#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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2prn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prn OCA], [https://pdbe.org/2prn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2prn RCSB], [https://www.ebi.ac.uk/pdbsum/2prn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2prn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PORI_FUSBL PORI_FUSBL] Forms channels that allow the passive diffusion of small hydrophilic solutes up to an exclusion limit of about 0.6 kDa.
== 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/pr/2prn_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=2prn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The general diffusion porin from Rhodopseudomonas blastica was produced in large amounts in Escherichia coli inclusion bodies and (re)natured to the exact native structure. Here, we report on 13 mutants at the pore eyelet giving rise to new diffusion properties as measured in planar lipid bilayer experiments. The crystal structures of seven of these mutants were established. The effects of charge-modifying mutations at the pore eyelet are consistent with the known selectivity for cations. Deletions of 16 and 27 residues of the constriction loop L3 resulted in labile trimers and pores. The reduction of the eyelet cross section by introducing tryptophans gave rise to a closely correlated decrease of the conductivities. A mutant with six newly introduced tryptophans in the eyelet closed its pore in a defined manner within seconds under a voltage of 20 mV, suggesting the existence of two states. The results indicate that the pore can be engineered in a rational manner.


==Overview==
Porin mutants with new channel properties.,Schmid B, Maveyraud L, Kromer M, Schulz GE Protein Sci. 1998 Jul;7(7):1603-11. PMID:9684893<ref>PMID:9684893</ref>
The general diffusion porin from Rhodopseudomonas blastica was produced in large amounts in Escherichia coli inclusion bodies and (re)natured to the exact native structure. Here, we report on 13 mutants at the pore eyelet giving rise to new diffusion properties as measured in planar lipid bilayer experiments. The crystal structures of seven of these mutants were established. The effects of charge-modifying mutations at the pore eyelet are consistent with the known selectivity for cations. Deletions of 16 and 27 residues of the constriction loop L3 resulted in labile trimers and pores. The reduction of the eyelet cross section by introducing tryptophans gave rise to a closely correlated decrease of the conductivities. A mutant with six newly introduced tryptophans in the eyelet closed its pore in a defined manner within seconds under a voltage of 20 mV, suggesting the existence of two states. The results indicate that the pore can be engineered in a rational manner.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2PRN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_blasticus Rhodobacter blasticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRN OCA].
</div>
<div class="pdbe-citations 2prn" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Porin mutants with new channel properties., Schmid B, Maveyraud L, Kromer M, Schulz GE, Protein Sci. 1998 Jul;7(7):1603-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9684893 9684893]
*[[Porin 3D structures|Porin 3D structures]]
[[Category: Rhodobacter blasticus]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Maveyraud, L.]]
__TOC__
[[Category: Schmid, B.]]
</StructureSection>
[[Category: Schulz, G E.]]
[[Category: Fuscovulum blasticum]]
[[Category: Integral membrane protein]]
[[Category: Large Structures]]
[[Category: Pore eyelet mutant]]
[[Category: Maveyraud L]]
[[Category: Porin]]
[[Category: Schmid B]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:41:16 2008''
[[Category: Schulz GE]]
Retrieved from "https://proteopedia.org/2prn"