FEBS Letters | |
The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution | |
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
【 预 览 】
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RO201912020294642ZK.pdf | 736KB | download |