2evu
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(New page: 200px<br /><applet load="2evu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2evu, resolution 2.3Å" /> '''Crystal structure of ...)
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Revision as of 08:03, 21 November 2007
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Crystal structure of aquaporin AqpM at 2.3A resolution
Overview
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.
About this Structure
2EVU is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with BOG and GOL as ligands. Full crystallographic information is available from OCA.
Reference
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
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