2iwv: Difference between revisions

Latest revision as of 10:51, 25 October 2023

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:	CA, LDA, TAM
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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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]

[2]

[3]

@@ 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: Difference between revisions

Latest revision as of 10:51, 25 October 2023

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

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