2f2b

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

spinqualitylabelsall models 2f2b, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2f2b is a 1 chain structure with sequence from Mettm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Related: 2evu Gene: aqpM (METTM) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AQPM_METTM] Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A.,Lee JK, Kozono D, Remis J, Kitagawa Y, Agre P, Stroud RM Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18932-7. Epub 2005 Dec 16. PMID:16361443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aquaporin 3D structures

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