3hyr
From Proteopedia
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| - | + | ==Structural Insight into G Protein Coupling and Regulation of Fe2+ Membrane Transport== | |
| - | + | <StructureSection load='3hyr' size='340' side='right' caption='[[3hyr]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3hyr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HYR FirstGlance]. <br> | |
| - | ==Function== | + | </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">[[3hyt|3hyt]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">feoB, b3409, JW3372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3hyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hyr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hyr RCSB], [http://www.ebi.ac.uk/pdbsum/3hyr PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/FEOB_ECOLI FEOB_ECOLI]] GTP-driven Fe(2+) uptake system.<ref>PMID:8407793</ref> <ref>PMID:12446835</ref> | [[http://www.uniprot.org/uniprot/FEOB_ECOLI FEOB_ECOLI]] GTP-driven Fe(2+) uptake system.<ref>PMID:8407793</ref> <ref>PMID:12446835</ref> | ||
| + | == 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/hy/3hyr_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes. | ||
| - | + | Structural basis of GDP release and gating in G protein coupled Fe2+ transport.,Guilfoyle A, Maher MJ, Rapp M, Clarke R, Harrop S, Jormakka M EMBO J. 2009 Sep 2;28(17):2677-85. Epub 2009 Jul 23. PMID:19629046<ref>PMID:19629046</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
| - | [[Category: Jormakka, M | + | [[Category: Jormakka, M]] |
| - | [[Category: Maher, M J | + | [[Category: Maher, M J]] |
[[Category: Cell inner membrane]] | [[Category: Cell inner membrane]] | ||
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
Revision as of 12:43, 25 December 2014
Structural Insight into G Protein Coupling and Regulation of Fe2+ Membrane Transport
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