6prn: Difference between revisions
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[[Image: | ==E1M, K50A, R52A MUTANT OF RH. BLASTICA PORIN== | ||
<StructureSection load='6prn' size='340' side='right' caption='[[6prn]], [[Resolution|resolution]] 2.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6prn]] 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=6PRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PRN 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> | |||
<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=6prn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6prn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=6prn RCSB], [http://www.ebi.ac.uk/pdbsum/6prn PDBsum]</span></td></tr> | |||
</table> | |||
== 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/6prn_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/chain_selection.php?pdb_ID=2ata 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Porin|Porin]] | *[[Porin|Porin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Rhodobacter blasticus]] | [[Category: Rhodobacter blasticus]] | ||
[[Category: Maveyraud, L | [[Category: Maveyraud, L]] | ||
[[Category: Schmid, B | [[Category: Schmid, B]] | ||
[[Category: Schulz, G E | [[Category: Schulz, G E]] | ||
[[Category: Integral membrane protein]] | [[Category: Integral membrane protein]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Pore eyelet mutant]] | [[Category: Pore eyelet mutant]] | ||
[[Category: Porin]] | [[Category: Porin]] | ||
Revision as of 20:01, 10 December 2014
E1M, K50A, R52A MUTANT OF RH. BLASTICA PORINE1M, K50A, R52A MUTANT OF RH. BLASTICA PORIN
Structural highlights
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 PubMedThe 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 AlsoReferences |
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