2f2b: Difference between revisions

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[[Image:2f2b.~~gif~~|left|200px]]

[[Image:2f2b.png|left|200px]]

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

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

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16361443}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16361443 is the PubMed ID number.

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==About this Structure==

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[[Category: Integral membrane protein]]

[[Category: Protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4~~ 03:22:52 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:43:31 2008''

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-[[Image:2f2b.gif|left|200px]]
+{{Seed}}
+[[Image:2f2b.png|left|200px]]
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 {{STRUCTURE_2f2b|  PDB=2f2b  |  SCENE=  }}
-'''Crystal structure of integral membrane protein Aquaporin AqpM at 1.68A resolution'''
+===Crystal structure of integral membrane protein Aquaporin AqpM at 1.68A 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16361443}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16361443 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16361443}}
 ==About this Structure==
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 [[Category: Integral membrane protein]]
 [[Category: Protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:22:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:43:31 2008''