6sly
From Proteopedia
(Difference between revisions)
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<StructureSection load='6sly' size='340' side='right'caption='[[6sly]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='6sly' size='340' side='right'caption='[[6sly]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6sly]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6sly]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EC544_07375 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [http://pdbe.org/6sly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [http://www.ebi.ac.uk/pdbsum/6sly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A0A438WSV6_HELPX A0A438WSV6_HELPX]] 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.[RuleBase:RU362123] | [[http://www.uniprot.org/uniprot/A0A438WSV6_HELPX A0A438WSV6_HELPX]] 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.[RuleBase:RU362123] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The growing understanding of partially unfolded proteins increasingly points to their biological relevance in allosteric regulation, complex formation, and protein design. However, the structural characterization of disordered proteins remains challenging. NMR methods can access both the dynamics and structures of such proteins, yet suffering from a high degeneracy of NMR signals. Here, we overcame this bottleneck utilizing a salt-inducible split intein to produce segmentally isotope-labeled samples with the native sequence, including the ligation junction. With this technique, we investigated the NMR structure and conformational dynamics of TonB from Helicobacter pylori in the presence of a proline-rich low complexity region. Spin relaxation experiments suggest that the several nano-second time scale dynamics of the C-terminal domain (CTD) is almost independent of the faster pico-to-nanosecond dynamics of the low complexity central region (LCCR). Our results demonstrate the utility of segmental isotopic labeling for proteins with heterogenous dynamics such as TonB and could advance NMR studies of other partially unfolded proteins. | ||
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| + | NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein.,Ciragan A, Backlund SM, Mikula KM, Beyer HM, Samuli Ollila OH, Iwai H Front Chem. 2020 Mar 19;8:136. doi: 10.3389/fchem.2020.00136. eCollection 2020. PMID:32266203<ref>PMID:32266203</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6sly" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 43504]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ciragan, A]] | [[Category: Ciragan, A]] | ||
Revision as of 07:17, 15 April 2020
NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-285)
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