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Structure–function correlation of outer membrane protein porin from Paracoccus denitrificans
Author(s) -
Sukumaran S.,
Hauser K.,
Maier E.,
Benz R.,
Mäntele W.
Publication year - 2006
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20422
Subject(s) - porin , paracoccus denitrificans , chemistry , bacterial outer membrane , biophysics , membrane , function (biology) , biochemistry , crystallography , stereochemistry , microbiology and biotechnology , escherichia coli , biology , gene , enzyme
Porins from outer membrane of Gram‐negative bacteria have a highly stable structure. Our previous studies on porin from Paracoccus denitrificans showed that the outer membrane protein porin is extremely stable toward heat, pH, and chemical denaturants. The major question we have addressed in this paper is whether the high stability of porin is a consequence of the β‐barrel structure and whether it is required for its function. To explain this we have analyzed two cases: first, we used porin wild‐type and mutants and compared their structure and function; second, we compared the activity of porin preheated to different temperatures. Structural changes were monitored by infrared spectroscopy. We observed that the structural stability of porin is not equivalent to functional activity as minor alteration in the structure can result in drastic differences in the activity of porins. © 2005 Wiley Periodicals, Inc. Biopolymers 82: 344–348, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com