6SLY

NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-285)

Summary for 6SLY

• Entry DOI: 10.2210/pdb6sly/pdb
• NMR Information: BMRB: 34425
• Descriptor: Protein TonB (1 entity in total)
• Functional Keywords: tonb-dependent iron uptake, c-terminal domain, metal transport
• Biological source: Helicobacter pylori
• Total number of polymer chains: 1
• Total formula weight: 11614.14

Authors

Ciragan, A.,Heikkinen, H.A.,Iwai, H. (deposition date: 2019-08-21, release date: 2020-03-25, Last modification date: 2024-02-28)

Primary citation

Ciragan, A.,Backlund, S.M.,Mikula, K.M.,Beyer, H.M.,Samuli Ollila, O.H.,Iwai, H.
NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein.
Front Chem, 8:136-136, 2020

PubMed Abstract: 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 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.

PubMed: 32266203
DOI: 10.3389/fchem.2020.00136

Experimental method

SOLUTION NMR