2evu

<StructureSection load='2evu' size='340' side='right' caption='[[2evu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[2evu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mettm Mettm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EVU FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2evu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evu OCA], [http://pdbe.org/2evu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2evu RCSB], [http://www.ebi.ac.uk/pdbsum/2evu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2evu ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/AQPM_METTM 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.

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== 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<ref>PMID:16361443</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2evu" style="background-color:#fffaf0;"></div>

*[[Aquaporin|Aquaporin]]

*[[Nobel Prizes for 3D Molecular Structure|Nobel Prizes for 3D Molecular Structure]]

[[Category: Mettm]]

[[Category: Agre, P]]

[[Category: CSMP, Center for Structures of Membrane Proteins]]

[[Category: Kitagawa, Y]]

[[Category: Kozono, D]]

[[Category: Lee, J K]]

[[Category: Remis, J]]

[[Category: Stroud, R M]]

[[Category: Structural genomic]]