Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å

John K. Lee, David Kozono, Jonathan Remis, Yoshichika Kitagawa, Peter Agre, Robert M. Stroud

Research output: Contribution to journalArticle

Abstract

To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis, we determined the structure of AqpM to 1.68-Å resolution by x-ray crystallography. The structure establishes AqpM as being in a unique subdivision between the two major subdivisions of aquaporins, the water-selective aquaporins, and the water-plus-glycerol- conducting aquaglyceroporins. In AqpM, isoleucine replaces a key histidine residue found in the lumen of water channels, which becomes a glycine residue in aquaglyceroporins. As a result of this and other side-chain substituents in the walls of the channel, the channel is intermediate in size and exhibits differentially tuned electrostatics when compared with the other subfamilies.

Original languageEnglish (US)
Pages (from-to)18932-18937
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number52
DOIs
StatePublished - Dec 27 2005

Keywords

  • Gas
  • Integral membrane protein
  • Water channel
  • X-ray crystallography

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å'. Together they form a unique fingerprint.

  • Cite this