A common channel-forming motif in evolutionarily distant porins.
Four new crystal packings of Escherichia coli porins are presented (phosphoporin, maltoporin, and two crystal forms of matrix porin). These were determined by molecular replacement methods using a polyalanine trial model acquired from the refined coordinates of porin from Rhodobacter capsulatus. The successful molecular replacement shows that the dominant motif found in R. capsulatus porin (a 16-stranded antiparallel beta-barrel) also applies to the E. coli porins, despite the lack of significant amino acid sequence homology. A 30 degrees-40 degrees tilt of the beta-strands with respect to the membrane normal was derived from the intensity distributions in the X-ray diffraction patterns for each porin studied, stressing their similarity. In view of the evolutionary distance between enteric and photosynthetic bacteria, the antiparallel beta-barrel may have significance as a basic structural motif for the formation of bacterial membrane channel structures.
Pauptit
R A
RA
Biocenter, University of Basel, Switzerland.
Schirmer
T
T
Jansonius
J N
JN
Rosenbusch
J P
JP
Parker
M W
MW
Tucker
A D
AD
Tsernoglou
D
D
Weiss
M S
MS
Schultz
G E
GE
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D005075:Biological Evolution; D003198:Computer Simulation; D003460:Crystallization; D004926:Escherichia coli / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry*; D008958:Models, Molecular; D018272:Porins; D016354:Rhodobacter capsulatus / Q000737:chemistry; D014961:X-Ray Diffraction
D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D018272:Porins