The structure of porin from Paracoccus denitrificans at 3.1 angstrom resolution

被引：50

作者：

Hirsch, A

Breed, J

Saxena, K

Richter, OMH

Ludwig, B

Diederichs, K

Welte, W

机构：

[1] UNIV KONSTANZ,FAK BIOL,D-78464 CONSTANCE,GERMANY

[2] UNIV FRANKFURT,INST BIOCHEM MOL GENET,D-60439 FRANKFURT,GERMANY

来源：

FEBS LETTERS | 1997年 / 404卷 / 2-3期

关键词：

porin; membrane protein structure; X-ray structure; molecular replacement; Paracoccus denitificans; ESCHERICHIA-COLI; CHANNEL;

D O I：

10.1016/S0014-5793(97)00131-2

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：

The crystal structure of a non-specific porin from Paracoccus denitrificans at 3.1 Angstrom resolution has been solved by molecular replacement using the porin from Rhodopseudomonas blastica as the search model. Paracoccus porin is very similar to other non-specific porins of known structure: a trimer of 16 stranded beta-barrels each with a central pore constricted by a long extracellular loop folding back against the barrel wall. The distinctive distribution of charged residues of this non-specific porin contributes to understanding the relation between structure and ion selectivity. (C) 1997 Federation of European Biochemical Societies.

引用

页码：208 / 210

页数：3

共 25 条

[21] X-ray crystallographic and mass spectrometric structure determination and functional characterization of succinylated porin from Rhodobacter capsulatus: Implications for ion selectivity and single-channel conductance [J].