2evu

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{{STRUCTURE_2evu| PDB=2evu | SCENE= }}
{{STRUCTURE_2evu| PDB=2evu | SCENE= }}
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'''Crystal structure of aquaporin AqpM at 2.3A resolution'''
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===Crystal structure of aquaporin AqpM at 2.3A resolution===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16361443 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16361443}}
==About this Structure==
==About this Structure==
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[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:19:41 2008''

Revision as of 14:19, 28 July 2008

Image:2evu.png

Template:STRUCTURE 2evu

Crystal structure of aquaporin AqpM at 2.3A resolution

Template:ABSTRACT PUBMED 16361443

About this Structure

2EVU is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. 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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