Vipp1 and PspA: Related but not twins

Jelle B. Bultema, Eva Fuhrmann, Egbert J. Boekema, Dirk Schneider

Research output: Contribution to journalArticleAcademicpeer-review

187 Downloads (Pure)


The Vesicle Inducing Protein in Plastids 1 (Vipp1) was suggested to be involved in thylakoid membrane formation in both chloroplasts and cyanobacteria. The protein shows sequence homology to the Phage Shock Protein A (PspA) from bacteria, and both proteins have similar secondary structures. 2D-structures of PspA and of Vipp1 have been determined by electron microscopy in the recent years. Both PspA and Vipp1 form large homooligomeric rings with high molecular masses but their ring dimensions differ significantly. Furthermore, Vipp1 forms rings with different rotational symmetries whereas PspA appears to form rings with singular rotational symmetry. In this article addendum we compare the structures of PspA and Vipp1. Furthermore, we suggest a spatial structural model of the observed Vipp1 rings.
Original languageEnglish
Pages (from-to)162-165
Number of pages4
JournalCommunicative & Integrative Biology
Issue number2
Publication statusPublished - 1-Mar-2010


  • function
  • structure
  • ring
  • Vipp1
  • PspA

Cite this