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This family consists of several bacterial proteins which are homologous to the oligogalacturonate-specific porin protein KdgM from Erwinia chrysanthemi. This phytopathogenic Gram-negative bacterium secretes pectinases, which are able to degrade the pectic polymers of plant cell walls and uses the degradation products as a carbon source for growth. KdgM is a Major Outer Membrane Protein (MOMP), whose synthesis is induced in the presence of the pectic derivatives. KdgM behaves like a voltage-dependent porin that is slightly selective for anions and that exhibits fast block in the presence of trigalacturonate. The family members seem to be monomeric, while the determined 3D structure of NanC porin suggests that they possess a 12-stranded ß-barrel, with rather short extracellular loops and a larger one that restricts the size of the pore.
Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli
J Bacteriol. 2005 Mar;187(6):1959-65. doi: 10.1128/JB.187.6.1959-1965.2005.
Topology of the Erwinia chrysanthemi oligogalacturonate porin KdgM
Biochem J. 2003 Jun 1;372(Pt 2):329-34. doi: 10.1042/BJ20030027.
The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family
J Biol Chem. 2002 Mar 8;277(10):7936-44. doi: 10.1074/jbc.M109193200. Epub 2001 Dec 28.
Projection maps of three members of the KdgM outer membrane protein family
J Struct Biol. 2007 Dec;160(3):395-403. doi: 10.1016/j.jsb.2007.08.007. Epub 2007 Aug 23.
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. doi: 10.1016/j.jmb.2009.09.054. Epub 2009 Sep 29.
|Proteins in this family with 3D-structure|