2wjr

From Proteopedia

(Difference between revisions)

Current revision

NanC porin structure in rhombohedral crystal form.

Structural highlights

2wjr is a 1 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 1.8Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NANC_ECOLI Outer membrane channel protein allowing the entry of N-acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host cell surfaces) into the bacteria (Probable). NanC proteins form high-conductance channels which are open at low membrane potentials and which have a weak anion selectivity.^[1]

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

Sialic acids are acidic sugars present mostly on vertebrate cell surfaces, which can be metabolized by bacteria and act as an inflammation signal. N-Acetylneuraminic acid, the most abundant sialic acid, can enter into Escherichia coli K12 through NanC, an N-acetylneuraminic acid-inducible outer-membrane channel. With its 215 residues, NanC belongs to the family of small monomeric KdgM-related porins. KdgM homologues are found in gammaproteobacteria, including major plant and human pathogens, and together they define a large family of putative acidic sugar/oligosaccharide transporters, which are as yet poorly characterized. Here, we present the first high-resolution structure of a KdgM family member. NanC folds into a 28-A-high, 12-stranded beta-barrel, resembling the beta-domain of autotransporter NalP and defining an open pore with an average radius of 3.3 A. The channel is lined by two strings of basic residues facing each other across the pore, a feature that appears largely conserved within the KdgM family and is likely to facilitate the diffusion of acidic oligosaccharides.

NanC crystal structure, a model for outer-membrane channels of the acidic sugar-specific KdgM porin family.,Wirth C, Condemine G, Boiteux C, Berneche S, Schirmer T, Peneff CM J Mol Biol. 2009 Dec 11;394(4):718-31. Epub 2009 Sep 29. PMID:19796645^[2]

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

References

↑ Condemine G, Berrier C, Plumbridge J, Ghazi A. Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli. J Bacteriol. 2005 Mar;187(6):1959-65. PMID:15743943 doi:http://dx.doi.org/187/6/1959
↑ Wirth C, Condemine G, Boiteux C, Berneche S, Schirmer T, Peneff CM. NanC crystal structure, a model for outer-membrane channels of the acidic sugar-specific KdgM porin family. J Mol Biol. 2009 Dec 11;394(4):718-31. Epub 2009 Sep 29. PMID:19796645 doi:10.1016/j.jmb.2009.09.054

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='2wjr' size='340' side='right'caption='[[2wjr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wjr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WJR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wjr]] is a 1 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=2WJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WJR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wjq|2wjq]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=2wjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wjr OCA], [https://pdbe.org/2wjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wjr RCSB], [https://www.ebi.ac.uk/pdbsum/2wjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wjr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/NANC_ECOLI NANC_ECOLI]] Outer membrane channel protein allowing the entry of N-acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host cell surfaces) into the bacteria (Probable). NanC proteins form high-conductance channels which are open at low membrane potentials and which have a weak anion selectivity.<ref>PMID:15743943</ref>
+[https://www.uniprot.org/uniprot/NANC_ECOLI NANC_ECOLI] Outer membrane channel protein allowing the entry of N-acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host cell surfaces) into the bacteria (Probable). NanC proteins form high-conductance channels which are open at low membrane potentials and which have a weak anion selectivity.<ref>PMID:15743943</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Condemine, G]]
+[[Category: Condemine G]]
-[[Category: Peneff, C M]]
+[[Category: Peneff CM]]
-[[Category: Schirmer, T]]
+[[Category: Schirmer T]]
-[[Category: Wirth, C]]
+[[Category: Wirth C]]
-[[Category: Beta-barrel]]
-[[Category: Carbohydrate transport]]
-[[Category: Cell membrane]]
-[[Category: Cell outer membrane]]
-[[Category: Ion transport]]
-[[Category: Kdgm family]]
-[[Category: Membrane]]
-[[Category: Membrane protein]]
-[[Category: Monomeric porin]]
-[[Category: Porin]]
-[[Category: Sialic acid translocation]]
-[[Category: Sugar transport]]
-[[Category: Transmembrane]]
-[[Category: Transport]]
-[[Category: Transport protein]]

2wjr

From Proteopedia

Current revision

NanC porin structure in rhombohedral crystal form.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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