scholarly journals Unusual Structural Features Revealed by the Solution NMR Structure of the NLRC5 Caspase Recruitment Domain

Biochemistry ◽  
2014 ◽  
Vol 53 (19) ◽  
pp. 3106-3117 ◽  
Author(s):  
Petrus G. M. Gutte ◽  
Simon Jurt ◽  
Markus G. Grütter ◽  
Oliver Zerbe
Keyword(s):  
Structural Features ◽  
Nmr Structure ◽  
Solution Nmr ◽  
Caspase Recruitment Domain

scholarly journals Intra-locked G-quadruplex structures formed by irregular DNA G-rich motifs

2020 ◽  
Vol 48 (6) ◽  
pp. 3315-3327 ◽  
Author(s):  
Arijit Maity ◽  
Fernaldo Richtia Winnerdy ◽  
Weili Denyse Chang ◽  
Gang Chen ◽  
Anh Tuân Phan
Keyword(s):  
Human Genome ◽  
Dna Sequences ◽  
Structural Features ◽  
Nmr Structure ◽  
Solution Nmr ◽  
Structural Studies ◽  
High Propensity ◽  
G Quadruplex ◽  
High Prevalence

Abstract G-rich DNA sequences with tracts of three or more continuous guanines (G≥3) are known to have high propensity to adopt stable G-quadruplex (G4) structures. Bioinformatic analyses suggest high prevalence of G-rich sequences with short G-tracts (G≤2) in the human genome. However, due to limited structural studies, the folding principles of such sequences remain largely unexplored and hence poorly understood. Here, we present the solution NMR structure of a sequence named AT26 consisting of irregularly spaced G2 tracts and two isolated single guanines. The structure is a four-layered G4 featuring two bi-layered blocks, locked between themselves in an unprecedented fashion making it a stable scaffold. In addition to edgewise and propeller-type loops, AT26 also harbors two V-shaped loops: a 2-nt V-shaped loop spanning two G-tetrad layers and a 0-nt V-shaped loop spanning three G-tetrad layers, which are named as VS- and VR-loop respectively, based on their distinct structural features. The intra-lock motif can be a basis for extending the G-tetrad core and a very stable intra-locked G4 can be formed by a sequence with G-tracts of various lengths including several G2 tracts. Findings from this study will aid in understanding the folding of G4 topologies from sequences containing irregularly spaced multiple short G-tracts.

Solution NMR structure of titin N2A region Ig domain I83 and its interaction with metal ions

2021 ◽  
pp. 166977
Author(s):  
Colleen Kelly ◽  
Nicola Pace ◽  
Matthew Gage ◽  
Mark Pfuhl
Keyword(s):  
Metal Ions ◽  
Nmr Structure ◽  
Solution Nmr ◽  
Ig Domain

scholarly journals Solution NMR Structure of the Ca2+-bound N-terminal Domain of CaBP7

2012 ◽  
Vol 287 (45) ◽  
pp. 38231-38243 ◽  
Author(s):  
Hannah V. McCue ◽  
Pryank Patel ◽  
Andrew P. Herbert ◽  
Lu-Yun Lian ◽  
Robert D. Burgoyne ◽  
...  
Keyword(s):  
Nmr Structure ◽  
Solution Nmr ◽  
Terminal Domain

scholarly journals NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e5412 ◽  
Author(s):  
Jesper S. Oeemig ◽  
O.H. Samuli Ollila ◽  
Hideo Iwaï
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Structural Changes ◽  
Nmr Structure ◽  
Dynamics Simulation ◽  
Solution Nmr ◽  
Gram Negative Bacteria ◽  
E Coli ◽  
Terminal Domain ◽  
Tonb Protein ◽  
Monomeric Structure

The TonB protein plays an essential role in the energy transduction system to drive active transport across the outer membrane (OM) using the proton-motive force of the cytoplasmic membrane of Gram-negative bacteria. The C-terminal domain (CTD) of TonB protein is known to interact with the conserved TonB box motif of TonB-dependent OM transporters, which likely induces structural changes in the OM transporters. Several distinct conformations of differently dissected CTDs of Escherichia coli TonB have been previously reported. Here we determined the solution NMR structure of a 96-residue fragment of Pseudomonas aeruginosa TonB (PaTonB-96). The structure shows a monomeric structure with the flexible C-terminal region (residues 338–342), different from the NMR structure of E. coli TonB (EcTonB-137). The extended and flexible C-terminal residues are confirmed by 15N relaxation analysis and molecular dynamics simulation. We created models for the PaTonB-96/TonB box interaction and propose that the internal fluctuations of PaTonB-96 makes it more accessible for the interactions with the TonB box and possibly plays a role in disrupting the plug domain of the TonB-dependent OM transporters.

scholarly journals Solution NMR structure of the N-terminal domain of the human DEK protein

2008 ◽  
Vol 17 (2) ◽  
pp. 205-215 ◽  
Author(s):  
Matthew Devany ◽  
Ferdinand Kappes ◽  
Kuan-Ming Chen ◽  
David M. Markovitz ◽  
Hiroshi Matsuo
Keyword(s):  
Nmr Structure ◽  
Solution Nmr ◽  
Terminal Domain

scholarly journals Structural insights into heme binding to IL-36α proinflammatory cytokine

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Amelie Wißbrock ◽  
Nishit B. Goradia ◽  
Amit Kumar ◽  
Ajay Abisheck Paul George ◽  
Toni Kühl ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Structural Investigation ◽  
Inflammatory Responses ◽  
Structural Features ◽  
Solution Nmr ◽  
Heme Binding ◽  
Structural Framework ◽  
Spectroscopic Analyses ◽  
Structural Insights ◽  
Fibroblast Like Synoviocytes

AbstractCytokines of the interleukin (IL)-1 family regulate immune and inflammatory responses. The recently discovered IL-36 family members are involved in psoriasis, rheumatoid arthritis, and pulmonary diseases. Here, we show that IL-36α interacts with heme thereby contributing to its regulation. Based on in-depth spectroscopic analyses, we describe two heme-binding sites in IL-36α that associate with heme in a pentacoordinated fashion. Solution NMR analysis reveals structural features of IL-36α and its complex with heme. Structural investigation of a truncated IL-36α supports the notion that the N-terminus is necessary for association with its cognate receptor. Consistent with our structural studies, IL-36-mediated signal transduction was negatively regulated by heme in synovial fibroblast-like synoviocytes from rheumatoid arthritis patients. Taken together, our results provide a structural framework for heme-binding proteins and add IL-1 cytokines to the group of potentially heme-regulated proteins.

scholarly journals Solution NMR Structure Investigation for Releasing Mechanism of Neocarzinostatin Chromophore from the Holoprotein

2005 ◽  
Vol 280 (12) ◽  
pp. 11340-11346 ◽  
Author(s):  
Hiroyuki Takashima ◽  
Takuya Yoshida ◽  
Tetsuya Ishino ◽  
Katsumi Hasuda ◽  
Tadayasu Ohkubo ◽  
...  
Keyword(s):  
Nmr Structure ◽  
Solution Nmr ◽  
Structure Investigation

Solution NMR Structure of Ribosome-binding Factor A (RbfA), A Cold-shock Adaptation Protein from Escherichia coli

2003 ◽  
Vol 327 (2) ◽  
pp. 521-536 ◽  
Author(s):  
Yuanpeng Janet Huang ◽  
G.V.T. Swapna ◽  
P.K. Rajan ◽  
Haiping Ke ◽  
Bing Xia ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cold Shock ◽  
Nmr Structure ◽  
Solution Nmr ◽  
Ribosome Binding ◽  
Binding Factor
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