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3hyt
From Proteopedia
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==Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+ Transport== | ==Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+ Transport== | ||
| - | <StructureSection load='3hyt' size='340' side='right' caption='[[3hyt]], [[Resolution|resolution]] 2.74Å' scene=''> | + | <StructureSection load='3hyt' size='340' side='right'caption='[[3hyt]], [[Resolution|resolution]] 2.74Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hyt]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3hyt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HYT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGO:2-AMINO-9-(5-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}PHOSPHORYL]-3-O-{[2-(METHYLAMINO)PHENYL]CARBONYL}-BETA-D-ERYTHRO-PENTOFURANOSYL-2-ULOSE)-1,9-DIHYDRO-6H-PURIN-6-ONE'>AGO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.74Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGO:2-AMINO-9-(5-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}PHOSPHORYL]-3-O-{[2-(METHYLAMINO)PHENYL]CARBONYL}-BETA-D-ERYTHRO-PENTOFURANOSYL-2-ULOSE)-1,9-DIHYDRO-6H-PURIN-6-ONE'>AGO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3hyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hyt OCA], [https://pdbe.org/3hyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hyt RCSB], [https://www.ebi.ac.uk/pdbsum/3hyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hyt ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FEOB_ECOLI FEOB_ECOLI] GTP-driven Fe(2+) uptake system.<ref>PMID:8407793</ref> <ref>PMID:12446835</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3hyt ConSurf]. | </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=3hyt ConSurf]. | ||
<div style="clear:both"></div> | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3hyt" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Jormakka M]] |
| - | [[Category: | + | [[Category: Maher MJ]] |
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Current revision
Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+ Transport
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