2F2B

Crystal structure of integral membrane protein Aquaporin AqpM at 1.68A resolution

Summary for 2F2B

• Entry DOI: 10.2210/pdb2f2b/pdb
• Related: 2evu
• Descriptor: Aquaporin aqpM, GLYCEROL (3 entities in total)
• Functional Keywords: protein, integral membrane protein, channel, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, membrane protein
• Biological source: Methanothermobacter marburgensis str. Marburg
• Cellular location: Cell membrane; Multi-pass membrane protein: Q9C4Z5
• Total number of polymer chains: 1
• Total formula weight: 25448.74

Authors

Lee, J.K.,Kozono, D.,Remis, J.,Kitagawa, Y.,Agre, P.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2005-11-15, release date: 2005-12-06, Last modification date: 2023-08-23)

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 (1.68 Å)