Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain.
Journal Article (Journal Article)
The cell division protein ZipA has an N-terminal transmembrane domain and a C-terminal globular domain that binds FtsZ. Between them are a charged domain and a P/Q domain rich in proline and glutamine that has been proposed to be an unfolded polypeptide. Here we provide evidence obtained by electron microscopy that the P/Q domain is a flexible tether ranging in length from 8 to 20 nm and invisible in rotary shadowing electron microscopy. We estimated a persistence length of 0.66 nm, which is similar to the persistence lengths of other unfolded and unstructured polypeptides.
Full Text
Duke Authors
Cited Authors
- Ohashi, T; Hale, CA; de Boer, PAJ; Erickson, HP
Published Date
- August 2002
Published In
Volume / Issue
- 184 / 15
Start / End Page
- 4313 - 4315
PubMed ID
- 12107152
Pubmed Central ID
- PMC135210
International Standard Serial Number (ISSN)
- 0021-9193
Digital Object Identifier (DOI)
- 10.1128/JB.184.15.4313-4315.2002
Language
- eng
Conference Location
- United States