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


  • eng

Conference Location

  • United States