2x9k: Difference between revisions

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[[Image:2x9k.png|left|200px]]
==STRUCTURE OF A E.COLI PORIN==
<StructureSection load='2x9k' size='340' side='right' caption='[[2x9k]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2x9k]] is a 1 chain structure with 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=2X9K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X9K FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wvp|2wvp]], [[2f1c|2f1c]], [[2iww|2iww]], [[2iwv|2iwv]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x9k RCSB], [http://www.ebi.ac.uk/pdbsum/2x9k PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The channel activity of the outer-membrane protein G (OmpG) from Escherichia coli is pH-dependent. To investigate the role of the histidine pair His231/His261 in triggering channel opening and closing, we mutated both histidines to alanines and cysteines. Fourier transform infrared spectra revealed that the OmpG mutants stay-independent of pH-in an open conformation. Temperature ramp experiments indicate that the mutants are as stable as the open state of wild-type OmpG. The X-ray structure of the alanine-substituted OmpG mutant obtained at pH 6.5 confirms the constitutively open conformation. Compared to previous structures of the wild-type protein in the open and closed conformation, the mutant structure shows a difference in the extracellular loop L6 connecting beta-strands S12 and S13. A deletion of amino acids 220-228, which are thought to block the channel at low pH in wild-type OmpG, indicates conformational changes, which might be triggered by His231/His261.


{{STRUCTURE_2x9k|  PDB=2x9k  |  SCENE=  }}
Correlation between the OmpG secondary structure and its pH-dependent alterations monitored by FTIR.,Korkmaz-Ozkan F, Koster S, Kuhlbrandt W, Mantele W, Yildiz O J Mol Biol. 2010 Aug 6;401(1):56-67. Epub 2010 Jun 16. PMID:20561532<ref>PMID:20561532</ref>


===STRUCTURE OF A E.COLI PORIN===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_20561532}}
 
==About this Structure==
[[2x9k]] is a 1 chain structure with 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=2X9K OCA].


==See Also==
==See Also==
*[[Porin|Porin]]
*[[Porin|Porin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020561532</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Korkmaz-Ozkan, F.]]
[[Category: Korkmaz-Ozkan, F.]]
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