1bh3: Difference between revisions

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==E1M, A116K MUTANT OF RH. BLASTICA PORIN==
==E1M, A116K MUTANT OF RH. BLASTICA PORIN==
<StructureSection load='1bh3' size='340' side='right' caption='[[1bh3]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
<StructureSection load='1bh3' size='340' side='right'caption='[[1bh3]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bh3]] is a 1 chain structure with 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=1BH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BH3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bh3]] 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=1BH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BH3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bh3 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh3 PDBsum]</span></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=1bh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh3 OCA], [https://pdbe.org/1bh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bh3 RCSB], [https://www.ebi.ac.uk/pdbsum/1bh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bh3 ProSAT]</span></td></tr>
</table>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bh3_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bh3_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1bh3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 24: Line 28:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 1bh3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Porin|Porin]]
*[[Porin 3D structures|Porin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Rhodobacter blasticus]]
[[Category: Fuscovulum blasticum]]
[[Category: Maveyraud, L]]
[[Category: Large Structures]]
[[Category: Schmid, B]]
[[Category: Maveyraud L]]
[[Category: Schulz, G E]]
[[Category: Schmid B]]
[[Category: Integral membrane protein]]
[[Category: Schulz GE]]
[[Category: Membrane protein]]
[[Category: Pore eyelet mutant]]
[[Category: Porin]]

Latest revision as of 14:01, 2 August 2023

E1M, A116K MUTANT OF RH. BLASTICA PORINE1M, A116K MUTANT OF RH. BLASTICA PORIN

Structural highlights

1bh3 is a 1 chain structure with sequence from Fuscovulum blasticum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.19Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

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.

Porin mutants with new channel properties.,Schmid B, Maveyraud L, Kromer M, Schulz GE Protein Sci. 1998 Jul;7(7):1603-11. PMID:9684893[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Schmid B, Maveyraud L, Kromer M, Schulz GE. Porin mutants with new channel properties. Protein Sci. 1998 Jul;7(7):1603-11. PMID:9684893

1bh3, resolution 2.19Å

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