2evu
From Proteopedia
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==Crystal structure of aquaporin AqpM at 2.3A resolution==  | ==Crystal structure of aquaporin AqpM at 2.3A resolution==  | ||
| - | <StructureSection load='2evu' size='340' side='right' caption='[[2evu]], [[Resolution|resolution]] 2.30Å' scene=''>  | + | <StructureSection load='2evu' size='340' side='right'caption='[[2evu]], [[Resolution|resolution]] 2.30Å' scene=''>  | 
== Structural highlights ==  | == Structural highlights ==  | ||
| - | <table><tr><td colspan='2'>[[2evu]] is a 1 chain structure with sequence from [  | + | <table><tr><td colspan='2'>[[2evu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_marburgensis_str._Marburg Methanothermobacter marburgensis str. Marburg]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2EVU FirstGlance]. <br>  | 
| - | </td></tr><tr id='  | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr>  | 
| - | <tr id='  | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[  | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2evu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evu OCA], [https://pdbe.org/2evu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2evu RCSB], [https://www.ebi.ac.uk/pdbsum/2evu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2evu ProSAT]</span></td></tr>  | 
</table>  | </table>  | ||
== Function ==  | == Function ==  | ||
| - | [  | + | [https://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.  | 
== Evolutionary Conservation ==  | == Evolutionary Conservation ==  | ||
[[Image:Consurf_key_small.gif|200px|right]]  | [[Image:Consurf_key_small.gif|200px|right]]  | ||
Check<jmol>  | Check<jmol>  | ||
  <jmolCheckbox>  |   <jmolCheckbox>  | ||
| - |     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/2evu_consurf.spt"</scriptWhenChecked>  | + |     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/2evu_consurf.spt"</scriptWhenChecked>  | 
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>  |     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>  | ||
    <text>to colour the structure by Evolutionary Conservation</text>  |     <text>to colour the structure by Evolutionary Conservation</text>  | ||
  </jmolCheckbox>  |   </jmolCheckbox>  | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/  | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2evu ConSurf].  | 
<div style="clear:both"></div>  | <div style="clear:both"></div>  | ||
| - | <div style="background-color:#fffaf0;">  | ||
| - | == 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.  | ||
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| - | 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>  | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | ||
| - | </div>  | ||
==See Also==  | ==See Also==  | ||
| - | *[[Aquaporin|Aquaporin  | + | *[[Aquaporin 3D structures|Aquaporin 3D structures]]  | 
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__TOC__  | __TOC__  | ||
</StructureSection>  | </StructureSection>  | ||
| - | [[Category:   | + | [[Category: Large Structures]]  | 
| - | [[Category:   | + | [[Category: Methanothermobacter marburgensis str. Marburg]]  | 
| - | [[Category:   | + | [[Category: Agre P]]  | 
| - | [[Category: Kitagawa  | + | [[Category: Kitagawa Y]]  | 
| - | [[Category: Kozono  | + | [[Category: Kozono D]]  | 
| - | [[Category: Lee  | + | [[Category: Lee JK]]  | 
| - | [[Category: Remis  | + | [[Category: Remis J]]  | 
| - | [[Category: Stroud  | + | [[Category: Stroud RM]]  | 
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Current revision
Crystal structure of aquaporin AqpM at 2.3A resolution
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