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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== |
| - | <StructureSection load='2f2b' size='340' side='right' caption='[[2f2b]], [[Resolution|resolution]] 1.68Å' scene=''> | + | <StructureSection load='2f2b' size='340' side='right'caption='[[2f2b]], [[Resolution|resolution]] 1.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f2b]] 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=2F2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F2B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2f2b]] 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=2F2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F2B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2evu|2evu]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aqpM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79929 METTM])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2b OCA], [https://pdbe.org/2f2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f2b RCSB], [https://www.ebi.ac.uk/pdbsum/2f2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f2b ProSAT]</span></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=2f2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2b OCA], [http://pdbe.org/2f2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f2b RCSB], [http://www.ebi.ac.uk/pdbsum/2f2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f2b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [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]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Aquaporin|Aquaporin]] | + | *[[Aquaporin 3D structures|Aquaporin 3D structures]] |
| - | *[[Nobel Prizes for 3D Molecular Structure|Nobel Prizes for 3D Molecular Structure]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mettm]] | + | [[Category: Large Structures]] |
| - | [[Category: Agre, P]] | + | [[Category: Methanothermobacter marburgensis str. Marburg]] |
| - | [[Category: CSMP, Center for Structures of Membrane Proteins]] | + | [[Category: Agre P]] |
| - | [[Category: Kitagawa, Y]] | + | [[Category: Kitagawa Y]] |
| - | [[Category: Kozono, D]] | + | [[Category: Kozono D]] |
| - | [[Category: Lee, J K]] | + | [[Category: Lee JK]] |
| - | [[Category: Remis, J]] | + | [[Category: Remis J]] |
| - | [[Category: Stroud, R M]] | + | [[Category: Stroud RM]] |
| - | [[Category: Center for structures of membrane protein]]
| + | |
| - | [[Category: Channel]]
| + | |
| - | [[Category: Csmp]]
| + | |
| - | [[Category: Integral membrane protein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Protein]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee JK, Kozono D, Remis J, Kitagawa Y, Agre P, Stroud RM. Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18932-7. Epub 2005 Dec 16. PMID:16361443
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