2pfu

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(New page: 200px<br /><applet load="2pfu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pfu" /> '''NMR strcuture determination of the periplasm...)
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[[Image:2pfu.jpg|left|200px]]<br /><applet load="2pfu" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pfu" />
 
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'''NMR strcuture determination of the periplasmic domain of ExbD from E.coli'''<br />
 
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==Overview==
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==NMR structure determination of the periplasmic domain of ExbD from E.coli==
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The transport of iron complexes through outer membrane transporters from, Gram-negative bacteria is highly dependent on the TonB system. Together, the three components of the system, TonB, ExbB and ExbD, energize the, transport of iron complexes through the outer membrane by utilizing the, proton motive force across the cytoplasmic membrane. The three-dimensional, (3D) structure of the periplasmic domain of TonB has previously been, determined. However, no detailed structural information for the other two, components of the TonB system is currently available and their role in the, iron-uptake process is not yet clearly understood. ExbD from Escherichia, coli contains 141 residues distributed in three domains: a small, N-terminal cytoplasmic region, a single transmembrane helix and a, C-terminal periplasmic domain. Here we describe the first well-defined, solution structure of the periplasmic domain of ExbD (residues 44-141), solved by multidimensional nuclear magnetic resonance (NMR) spectroscopy., The monomeric structure presents three clearly distinct regions: an, N-terminal flexible tail (residues 44-63), a well-defined folded region, (residues 64-133) followed by a small C-terminal flexible region (residues, 134-141). The folded region is formed by two alpha-helices that are, located on one side of a single beta-sheet. The central beta-sheet is, composed of five beta-strands, with a mixed parallel and antiparallel, arrangement. Unexpectedly, this fold closely resembles that found in the, C-terminal lobe of the siderophore-binding proteins FhuD and CeuE. The, ExbD periplasmic domain has a strong tendency to aggregate in vitro and, 3D-TROSY (transverse relaxation optimized spectroscopy) NMR experiments of, the deuterated protein indicate that the multimeric protein has nearly, identical secondary structure to that of the monomeric form. Chemical, shift perturbation studies suggest that the Glu-Pro region (residues, 70-83) of TonB can bind weakly to the surface and the flexible C-terminal, region of ExbD. At the same time the Lys-Pro region (residues 84-102) and, the folded C-terminal domain (residues 150-239) of TonB do not show, significant binding to ExbD, suggesting that the main interactions forming, the TonB complex occur in the cytoplasmic membrane.
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<StructureSection load='2pfu' size='340' side='right'caption='[[2pfu]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2pfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PFU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pfu OCA], [https://pdbe.org/2pfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pfu RCSB], [https://www.ebi.ac.uk/pdbsum/2pfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pfu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EXBD_ECOLI EXBD_ECOLI] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pf/2pfu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2pfu ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2PFU is a [http://en.wikipedia.org/wiki/Single_protein 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=2PFU OCA].
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*[[ExbD|ExbD]]
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__TOC__
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==Reference==
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</StructureSection>
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The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins., Garcia-Herrero A, Peacock RS, Howard SP, Vogel HJ, Mol Microbiol. 2007 Oct 10;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17927700 17927700]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Garcia-Herrero A]]
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[[Category: Garcia-Herrero, A.]]
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[[Category: Howard PS]]
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[[Category: Howard, P.S.]]
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[[Category: Peacock SR]]
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[[Category: Peacock, S.R.]]
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[[Category: Vogel HJ]]
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[[Category: Vogel, H.J.]]
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[[Category: exbd]]
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[[Category: periplasmic domain]]
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[[Category: proton motive force]]
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[[Category: tonb system]]
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[[Category: transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:04:46 2008''
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Current revision

NMR structure determination of the periplasmic domain of ExbD from E.coli

PDB ID 2pfu

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