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| | ==NMR solution structure of Helicobacter pylori TonB-CTD (residues 194-285)== | | ==NMR solution structure of Helicobacter pylori TonB-CTD (residues 194-285)== |
| - | <StructureSection load='5lw8' size='340' side='right'caption='[[5lw8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5lw8' size='340' side='right'caption='[[5lw8]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lw8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LW8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LW8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lw8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LW8 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tonB, HP_1341 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | + | </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=5lw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lw8 OCA], [https://pdbe.org/5lw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lw8 RCSB], [https://www.ebi.ac.uk/pdbsum/5lw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lw8 ProSAT]</span></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=5lw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lw8 OCA], [http://pdbe.org/5lw8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lw8 RCSB], [http://www.ebi.ac.uk/pdbsum/5lw8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lw8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TONB_HELPY TONB_HELPY]] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity). | + | [https://www.uniprot.org/uniprot/TONB_HELPY TONB_HELPY] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aranko, A S]] | + | [[Category: Aranko AS]] |
| - | [[Category: Ciragan, A]] | + | [[Category: Ciragan A]] |
| - | [[Category: Iwai, H]] | + | [[Category: Iwai H]] |
| - | [[Category: Tascon, I]] | + | [[Category: Tascon I]] |
| - | [[Category: C-terminal domain]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Proline rich domain]]
| + | |
| - | [[Category: Tonb-dependent iron uptake]]
| + | |
| Structural highlights
Function
TONB_HELPY Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).
Publication Abstract from PubMed
Intervening protein sequences (inteins) from extremely halophilic haloarchaea can be inactive under low salinity but could be activated by increasing salt contents to a specific concentration for each intein. The halo-obligatory inteins confer high solubility under both low and high salinity conditions. We showed the broad utility of salt-dependent protein splicing in cis and trans by demonstrating backbone cyclization, self-cleavage for purification, and scarless protein ligation for segmental isotopic labeling. Artificially split MCM2 intein derived from Halorhabdus utahensis remained highly soluble and was capable of protein trans-splicing with excellent ligation kinetics by reassembly under high salinity conditions. Importantly, the MCM2 intein has the active site residue of Ser at the +1 position, which remains in the ligated product, instead of Cys as found in many other efficient split inteins. Since Ser is more abundant than Cys in proteins, the novel split intein could widen applications of segmental labeling in protein NMR spectroscopy and traceless protein ligation by exploiting a Ser residue in the native sequences as the +1 position of the MCM2 intein. The split halo-obligatory intein was successfully used to demonstrate the utility in NMR investigation of intact proteins by producing segmentally isotope-labeled intact TonB protein from Helicobacter pylori.
Salt-inducible protein splicing in cis and trans by inteins from extremely halophilic archaea as a novel protein-engineering tool.,Ciragan A, Aranko AS, Tascon I, Iwai H J Mol Biol. 2016 Oct 6. pii: S0022-2836(16)30421-1. doi:, 10.1016/j.jmb.2016.10.006. PMID:27720988[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ciragan A, Aranko AS, Tascon I, Iwai H. Salt-inducible protein splicing in cis and trans by inteins from extremely halophilic archaea as a novel protein-engineering tool. J Mol Biol. 2016 Oct 6. pii: S0022-2836(16)30421-1. doi:, 10.1016/j.jmb.2016.10.006. PMID:27720988 doi:http://dx.doi.org/10.1016/j.jmb.2016.10.006
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