2iwv

From Proteopedia

(Difference between revisions)

Current revision

Structure of the monomeric outer membrane porin OmpG in the open and closed conformation

Structural highlights

2iwv is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OMPG_ECOLI Forms channels functionally larger than those of classical porins.^[1] May act as a regulator of the RCS-phosphorelay signal transduction pathway.^[2]

Publication Abstract from PubMed

OmpG, a monomeric pore-forming protein from Escherichia coli outer membranes, was refolded from inclusion bodies and crystallized in two different conformations. The OmpG channel is a 14-stranded beta-barrel, with short periplasmic turns and seven extracellular loops. Crystals grown at neutral pH show the channel in the open state at 2.3 A resolution. In the 2.7 A structure of crystals grown at pH 5.6, the pore is blocked by loop 6, which folds across the channel. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues. A total of 151 ordered LDAO detergent molecules were found in the 2.3 A structure, mostly on the hydrophobic outer surface of OmpG, mimicking the outer membrane lipid bilayer, with three LDAO molecules in the open pore. In the 2.7 A structure, OmpG binds one OG and one glucose molecule as sugar substrates in the closed pore.

Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation.,Yildiz O, Vinothkumar KR, Goswami P, Kuhlbrandt W EMBO J. 2006 Aug 9;25(15):3702-13. Epub 2006 Aug 3. PMID:16888630^[3]

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

References

↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
↑ Yildiz O, Vinothkumar KR, Goswami P, Kuhlbrandt W. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J. 2006 Aug 9;25(15):3702-13. Epub 2006 Aug 3. PMID:16888630

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iwv"

@@ Line 1: / Line 1: @@
-==STRUCTURE OF THE MONOMERIC OUTER MEMBRANE PORIN OMPG IN THE OPEN AND CLOSED CONFORMATION==
-<StructureSection load='2iwv' size='340' side='right' caption='[[2iwv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+==Structure of the monomeric outer membrane porin OmpG in the open and closed conformation==
+<StructureSection load='2iwv' size='340' side='right'caption='[[2iwv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iwv]] is a 4 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=2IWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IWV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iwv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f1c|2f1c]], [[2iww|2iww]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=2iwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2iwv RCSB], [http://www.ebi.ac.uk/pdbsum/2iwv PDBsum]</span></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=2iwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwv OCA], [https://pdbe.org/2iwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwv RCSB], [https://www.ebi.ac.uk/pdbsum/2iwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwv ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/OMPG_ECOLI OMPG_ECOLI] Forms channels functionally larger than those of classical porins.<ref>PMID:11758943</ref>   May act as a regulator of the RCS-phosphorelay signal transduction pathway.<ref>PMID:11758943</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2iwv" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Porin|Porin]]
+*[[Porin 3D structures|Porin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Escherichia coli K-12]]
-[[Category: Goswami, P]]
+[[Category: Large Structures]]
-[[Category: Kuehlbrandt, W]]
+[[Category: Goswami P]]
-[[Category: Vinothkumar, K R]]
+[[Category: Kuehlbrandt W]]
-[[Category: Yildiz, O]]
+[[Category: Vinothkumar KR]]
-[[Category: Ion channel]]
+[[Category: Yildiz O]]
-[[Category: Ion transport]]
-[[Category: Membrane]]
-[[Category: Outer membrane]]
-[[Category: Porin]]
-[[Category: Transmembrane]]
-[[Category: Transport]]

2iwv

From Proteopedia

Current revision

Structure of the monomeric outer membrane porin OmpG in the open and closed conformation

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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