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3m7l
From Proteopedia
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| - | {{STRUCTURE_3m7l| PDB=3m7l | SCENE= }} | ||
| - | ===Crystal Structure of Plant SLAC1 homolog TehA=== | ||
| - | {{ABSTRACT_PUBMED_20981093}} | ||
| - | == | + | ==Crystal Structure of Plant SLAC1 homolog TehA== |
| - | [[3m7l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <StructureSection load='3m7l' size='340' side='right' caption='[[3m7l]], [[Resolution|resolution]] 1.50Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3m7l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M7L 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></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m71|3m71]], [[3m72|3m72]], [[3m73|3m73]], [[3m74|3m74]], [[3m75|3m75]], [[3m76|3m76]], [[3m77|3m77]], [[3m78|3m78]], [[3m7b|3m7b]], [[3m7c|3m7c]], [[3m7e|3m7e]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HI0511, Rd, tehA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</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=3m7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7l OCA], [http://pdbe.org/3m7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m7l RCSB], [http://www.ebi.ac.uk/pdbsum/3m7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TEHA_HAEIN TEHA_HAEIN]] Ion channel involved in potassium tellurite resistance. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/3m7l_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=3m7l ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The plant SLAC1 anion channel controls turgor pressure in the aperture-defining guard cells of plant stomata, thereby regulating the exchange of water vapour and photosynthetic gases in response to environmental signals such as drought or high levels of carbon dioxide. Here we determine the crystal structure of a bacterial homologue (Haemophilus influenzae) of SLAC1 at 1.20 A resolution, and use structure-inspired mutagenesis to analyse the conductance properties of SLAC1 channels. SLAC1 is a symmetrical trimer composed from quasi-symmetrical subunits, each having ten transmembrane helices arranged from helical hairpin pairs to form a central five-helix transmembrane pore that is gated by an extremely conserved phenylalanine residue. Conformational features indicate a mechanism for control of gating by kinase activation, and electrostatic features of the pore coupled with electrophysiological characteristics indicate that selectivity among different anions is largely a function of the energetic cost of ion dehydration. | ||
| - | + | Homologue structure of the SLAC1 anion channel for closing stomata in leaves.,Chen YH, Hu L, Punta M, Bruni R, Hillerich B, Kloss B, Rost B, Love J, Siegelbaum SA, Hendrickson WA Nature. 2010 Oct 28;467(7319):1074-80. PMID:20981093<ref>PMID:20981093</ref> | |
| - | <ref | + | |
| - | [[Category: | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[Category: Chen, Y H | + | </div> |
| - | [[Category: Hendrickson, W A | + | <div class="pdbe-citations 3m7l" style="background-color:#fffaf0;"></div> |
| - | [[Category: NYCOMPS, New York Consortium on Membrane Protein Structure | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacterium influenzae lehmann and neumann 1896]] | ||
| + | [[Category: Chen, Y H]] | ||
| + | [[Category: Hendrickson, W A]] | ||
| + | [[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]] | ||
[[Category: Alpha helical integral membrane protein]] | [[Category: Alpha helical integral membrane protein]] | ||
[[Category: Anion channel]] | [[Category: Anion channel]] | ||
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[[Category: Nycomp]] | [[Category: Nycomp]] | ||
[[Category: Plant slac-1 homolog]] | [[Category: Plant slac-1 homolog]] | ||
| - | [[Category: Protein structure initiative | + | [[Category: PSI, Protein structure initiative]] |
| - | + | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Current revision
Crystal Structure of Plant SLAC1 homolog TehA
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Categories: Bacterium influenzae lehmann and neumann 1896 | Chen, Y H | Hendrickson, W A | NYCOMPS, New York Consortium on Membrane Protein Structure | Alpha helical integral membrane protein | Anion channel | New york consortium on membrane protein structure | Nycomp | Plant slac-1 homolog | PSI, Protein structure initiative | Structural genomic | Unknown function
