A COMMON CHANNEL-FORMING MOTIF IN EVOLUTIONARILY DISTANT PORINS

被引:42
作者
PAUPTIT, RA
SCHIRMER, T
JANSONIUS, JN
ROSENBUSCH, JP
PARKER, MW
TUCKER, AD
TSERNOGLOU, D
WEISS, MS
SCHULZ, GE
机构
[1] EUROPEAN MOLEC BIOL LAB,W-6900 HEIDELBERG,GERMANY
[2] UNIV FREIBURG,INST ORGAN CHEM & BIOCHEM,W-7800 FREIBURG,GERMANY
关键词
D O I
10.1016/1047-8477(91)90017-Q
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 (β-barrel) also applies to the E. coli porins, despite the lack of significant amino acid sequence homology. A 30°-40° tilt of the β-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 β-barrel may have significance as a basic structural motif for the formation of bacterial membrane channel structures. © 1991.
引用
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页码:136 / 145
页数:10
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