2evu
From Proteopedia
(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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| - | [[Image:2evu.gif|left|200px]]<br /><applet load="2evu" size=" | + | [[Image:2evu.gif|left|200px]]<br /><applet load="2evu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2evu, resolution 2.3Å" /> | caption="2evu, resolution 2.3Å" /> | ||
'''Crystal structure of aquaporin AqpM at 2.3A resolution'''<br /> | '''Crystal structure of aquaporin AqpM at 2.3A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To explore the structural basis of the unique selectivity spectrum and | + | 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== | ==About this Structure== | ||
| - | 2EVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with BOG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2EVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=BOG:'>BOG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kitagawa, Y.]] | [[Category: Kitagawa, Y.]] | ||
[[Category: Kozono, D.]] | [[Category: Kozono, D.]] | ||
| - | [[Category: Lee, J | + | [[Category: Lee, J K.]] |
[[Category: Remis, J.]] | [[Category: Remis, J.]] | ||
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
[[Category: BOG]] | [[Category: BOG]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: alpha-helical]] | [[Category: alpha-helical]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:02 2008'' |
Revision as of 15:15, 21 February 2008
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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 and 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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