Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 305, Issue 1, Pages 71-77Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1006/jmbi.2000.4284
Keywords
electron crystallography; 2-D crystals; membrane protein; porin; beta-barrel
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The Escherichia coli porin OmpG, which acts as an efficient unspecific channel for mono-, di- and trisaccharides, has been purified and crystallized in two dimensions. Projection maps of two different crystal forms of OmpG at 6 Angstrom resolution show that the protein has a beta -barrel structure characteristic for outer membrane proteins, and that it does not form trimers, unlike most other porins such as OmpF and OmpC, but appears in monomeric form. The size of the barrel is similar to2.5 nm, indicating that OmpG may consist of 14 beta -strands. The projection map suggests that the channel is restricted by internal loops. (C) 2001 Academic Press.
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