2EVU

Crystal structure of aquaporin AqpM at 2.3A resolution

Summary for 2EVU

• Entry DOI: 10.2210/pdb2evu/pdb
• Descriptor: Aquaporin aqpM, octyl beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
• Functional Keywords: alpha-helical, membrane protein, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp
• Biological source: Methanothermobacter marburgensis str. Marburg
• Cellular location: Cell membrane; Multi-pass membrane protein: Q9C4Z5
• Total number of polymer chains: 1
• Total formula weight: 26493.94

Authors

Lee, J.K.,Kozono, D.,Remis, J.,Kitagawa, Y.,Agre, P.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2005-10-31, release date: 2005-12-06, Last modification date: 2024-02-14)

Primary citation

Lee, J.K.,Kozono, D.,Remis, J.,Kitagawa, Y.,Agre, P.,Stroud, R.M.
Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A.
Proc.Natl.Acad.Sci.Usa, 102:18932-18937, 2005

PubMed 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-A 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.

PubMed: 16361443
DOI: 10.1073/pnas.0509469102

Experimental method

X-RAY DIFFRACTION (2.3 Å)