The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution

FEBS Letters

Welte, W.¹  Nestel, U.¹  Weiss, M.S.²  Schulz, G.E.²  Kreusch, A.²  Schiltz, E.²  Weckesser, J.³ 

[1] Institut für Biophysik und Strahlenbiologie der Universität, Albertstr. 23, D-7800 Freiburg i. Br., Germany;Institut für Organische Chemie und Biochemie der Universität, Albertstr. 21, D-7800 Freiburg i. Br., Germany;Institut für Biologie II, Mikrobiologie der Universität, Schänzlestr, 1, D-7800 Freiburg i. Br., Germany

关键词: Porin;    Membrane channel structure;    β-Barrel topology;    X-Ray structure;    Rhodobacter capsulatus;   

DOI  :  10.1016/0014-5793(91)80336-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of the porin from Rhodobacter capsulanus was determined at a resolution of 1.8 Å. The analysis started from a closely related crystal structure that had been solved at a medium resolution of 3 Å using multiple isomorphous replacement and solvent flattening. The new structure contains the complete sequence of 301 amino acid residues. Refinement of the model is under way: the present R-factor is 22% with good geometry. Except for the lengths of several loops, the resulting chain fold corresponds to the medium resolution model. The membrane channel is lined by a large number of ionogenic side chains with characteristic segregation of differently charged groups.

【 授权许可】

Unknown