View source for 4pr7


==KdgM porin in complex with disordered oligogalacturonate==
<StructureSection load='4pr7' size='340' side='right'caption='[[4pr7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pr7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cfbp_1269 Cfbp 1269]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PR7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</scene>, <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fqe|4fqe]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kdgM, Dda3937_03362 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204038 CFBP 1269])</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=4pr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pr7 OCA], [http://pdbe.org/4pr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pr7 RCSB], [http://www.ebi.ac.uk/pdbsum/4pr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pr7 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/KDGM_DICD3 KDGM_DICD3]] Porin specific for oligogalacturonides. Also required for full virulence. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phytopathogenic Gram-negative bacterium Dickeya dadantii (Erwinia chrysanthemi) feeds on plant cell walls by secreting pectinases and utilizing the oligogalacturanate products. An outer membrane porin, KdgM, is indispensable for the uptake of these acidic oligosaccharides. Here, the crystal structure of KdgM determined to 1.9 A resolution is presented. KdgM is folded into a regular 12-stranded antiparallel beta-barrel with a circular cross-section defining a transmembrane pore with a minimal radius of 3.1 A. Most of the loops that would face the cell exterior in vivo are disordered, but nevertheless mediate contact between densely packed membrane-like layers in the crystal. The channel is lined by two tracks of arginine residues facing each other across the pore, a feature that is conserved within the KdgM family and is likely to facilitate the diffusion of acidic oligosaccharides.

Structure of the oligogalacturonate-specific KdgM porin.,Hutter CA, Lehner R, Wirth Ch, Condemine G, Peneff C, Schirmer T Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1770-8. doi:, 10.1107/S1399004714007147. Epub 2014 May 30. PMID:24914987<ref>PMID:24914987</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pr7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Porin|Porin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cfbp 1269]]
[[Category: Large Structures]]
[[Category: Hutter, C]]
[[Category: Peneff, C M]]
[[Category: Schirmer, T]]
[[Category: Wirth, C]]
[[Category: Beta barrel]]
[[Category: Oligogalacturonate specificity]]
[[Category: Outer membrane protein]]
[[Category: Transport protein]]