The three‐dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution

FEBS Letters

Weiss, M.S.²  Schulz, G.E.²  Wacker, T.³  Weite, W.³  Weckesser, J.¹ 

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

关键词: Porin;    Membrane protein structure;    X-ray structure;    Rhodobacter capsulatus;   

DOI  :  10.1016/0014-5793(90)80942-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of porin from Rhodobacter capsulatus strain 37b4 has been solved at 3.0 Å (1 Å = 0.1 nm) resolution by multiple isomorphous replacement and solvent-flattening. The three pores of the trimer are well denned in the electron density map. Each pore consists of a 16-stranded β-barrel which traverses the membrane as a tube. Near its center the tube is narrowed by chain segments protruding from the inner wall of the barrel that form an eye-let with an irregular cross-section of about 6 Å by 10 Å. The eye-let has an axial length of about 10 Å; it defines the exclusion limit for diffusing particles.

【 授权许可】

Unknown