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| - | [[Image:2d1u.gif|left|200px]] | |
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| - | {{Structure
| + | ==Solution structure of the periplasmic signaling domain of FecA from Escherichia coli== |
| - | |PDB= 2d1u |SIZE=350|CAPTION= <scene name='initialview01'>2d1u</scene>
| + | <StructureSection load='2d1u' size='340' side='right'caption='[[2d1u]]' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[2d1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D1U FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | |GENE= fecA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1u OCA], [https://pdbe.org/2d1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d1u RCSB], [https://www.ebi.ac.uk/pdbsum/2d1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d1u ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY= | + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1u OCA], [http://www.ebi.ac.uk/pdbsum/2d1u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d1u RCSB]</span>
| + | [https://www.uniprot.org/uniprot/FECA_ECOLI FECA_ECOLI] FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system. |
| - | }}
| + | == Evolutionary Conservation == |
| - | | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | '''Solution strcuture of the periplasmic signaling domain of FecA from Escherichia coli'''
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d1/2d1u_consurf.spt"</scriptWhenChecked> |
| - | ==Overview== | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | Gram-negative bacteria possess outer membrane receptors that utilize energy provided by the TonB system to take up iron. Several of these receptors participate in extracytoplasmic factor (ECF) signalling through an N-terminal signalling domain that interacts with a periplasmic transmembrane anti-sigma factor protein and a cytoplasmic sigma factor protein. The structures of the intact TonB-dependent outer membrane receptor FecA from Escherichia coli and FpvA from Pseudomonas aeruginosa have recently been solved by protein crystallography; however, no electron density was detected for their periplasmic signalling domains, suggesting that it was either unfolded or flexible with respect to the remainder of the protein. Here we describe the well-defined solution structure of this domain solved by multidimensional nuclear magnetic resonance (NMR) spectroscopy. The monomeric protein construct contains the 79-residue N-terminal domain as well as the next 17 residues that are part of the receptor's plug domain. These form two clearly distinct regions: a highly structured domain at the N-terminal end followed by an extended flexible tail at the C-terminal end, which includes the 'TonB-box' region, and connects it to the plug domain of the receptor. The structured region consists of two alpha-helices that are positioned side by side and are sandwiched in between two small beta-sheets. This is a novel protein fold which appears to be preserved in all the periplasmic signalling domains of bacterial TonB-dependent outer membrane receptors that are involved in ECF signalling, because the hydrophobic residues that make up the core of the protein domain are highly conserved.
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | | + | </jmolCheckbox> |
| - | ==About this Structure== | + | </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=2d1u ConSurf]. |
| - | 2D1U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1U OCA].
| + | <div style="clear:both"></div> |
| - | | + | __TOC__ |
| - | ==Reference==
| + | </StructureSection> |
| - | Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli., Garcia-Herrero A, Vogel HJ, Mol Microbiol. 2005 Dec;58(5):1226-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16313612 16313612]
| + | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Garcia-Herrero, A.]] | + | [[Category: Garcia-Herrero A]] |
| - | [[Category: Vogel, H J.]] | + | [[Category: Vogel HJ]] |
| - | [[Category: feca]]
| + | |
| - | [[Category: iron-uptake]]
| + | |
| - | [[Category: surface signaling]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:09 2008''
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