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Comment
. 2007 May 15;104(20):8199-200.
doi: 10.1073/pnas.0702745104. Epub 2007 May 9.

From rhomboid function to structure and back again

Raquel L Lieberman  1 , Michael S Wolfe
Affiliations
Comment

From rhomboid function to structure and back again

Raquel L Lieberman et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Escherichia coli rhomboid GlpG structure and effects of mutations on enzyme activity. Cartoon representations of GlpG monomers are from Protein Data Bank ID code 2NRF, with relevant residues highlighted in yellow ball-and-stick. Orientation is parallel to membrane normal (a Left, b, d, and e) and perpendicular (a Right and c). −, decreased activity; X, abolished activity; +, enhanced activity. (a) Overall rhomboid topology and location of the active site. (b) Mutations that perturb L1–lipid interactions impair activity. (c) Disruption of L1–core TM helix interactions decreases activity. (d) All mutations in the active site lead to abolished activity. (e) Enhancing access at TM2–TM5 interface increases activity, and closing access via disulfide linkages (red) decreases activity.
See this image and copyright information in PMC

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