scholarly journals The NMR solution structure of the 30S ribosomal protein S27e encoded in geneRS27_ARCFUofArchaeoglobus fulgidisreveals a novel protein fold

2004 ◽  
Vol 13 (5) ◽  
pp. 1407-1416 ◽  
Author(s):  
Catherine Herve du Penhoat ◽  
Hanudatta S. Atreya ◽  
Yang Shen ◽  
Gaohua Liu ◽  
Thomas B. Acton ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Solution Structure ◽  
Protein Fold ◽  
Nmr Solution Structure ◽  
Novel Protein

NMR Solution Structure of the Archaebacterial Chromosomal Protein MC1 Reveals a New Protein Fold‡

Biochemistry ◽  
2004 ◽  
Vol 43 (47) ◽  
pp. 14971-14978 ◽  
Author(s):  
Françoise Paquet ◽  
Françoise Culard ◽  
Florent Barbault ◽  
Jean-Claude Maurizot ◽  
Gérard Lancelot
Keyword(s):  
Solution Structure ◽  
Chromosomal Protein ◽  
Protein Fold ◽  
Nmr Solution Structure ◽  
New Protein

Structure determination of archaea-specific ribosomal protein L46a reveals a novel protein fold

2014 ◽  
Vol 450 (1) ◽  
pp. 67-72 ◽  
Author(s):  
Yingang Feng ◽  
Xiaxia Song ◽  
Jinzhong Lin ◽  
Jinsong Xuan ◽  
Qiu Cui ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Structure Determination ◽  
Protein Fold ◽  
Novel Protein

scholarly journals A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc

Metallomics ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 1415-1429 ◽  
Author(s):  
Jelena Habjanič ◽  
Oliver Zerbe ◽  
Eva Freisinger
Keyword(s):  
Solution Structure ◽  
Binding Capacity ◽  
Metal Cluster ◽  
Protein Fold ◽  
Nmr Solution Structure

The NMR solution structure of a Pseudomonas metallothionein reveals a different binding capacity for ZnII and CdII ions that results in two novel metal-cluster topologies. Replacement of a non-coordinating residue by histidine decreases the kinetic lability of the cluster. All three structures reported show an identical protein fold.

scholarly journals Structural Basis for the C-Terminal Domain of Mycobacterium tuberculosis Ribosome Maturation Factor RimM to Bind Ribosomal Protein S19

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 597
Author(s):  
Haoran Zhang ◽  
Qiuxiang Zhou ◽  
Chenyun Guo ◽  
Liubin Feng ◽  
Huilin Wang ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Solution Structure ◽  
Molecular Mechanisms ◽  
Structural Model ◽  
Ribosomal Subunit ◽  
Structural Basis ◽  
Hydrophobic Core ◽  
Terminal Domain ◽  
Ribosomal Protein S19

Multidrug-resistant tuberculosis (TB) is a serious threat to public health, calling for the development of new anti-TB drugs. Chaperon protein RimM, involved in the assembly of ribosomal protein S19 into 30S ribosomal subunit during ribosome maturation, is a potential drug target for TB treatment. The C-terminal domain (CTD) of RimM is primarily responsible for binding S19. However, both the CTD structure of RimM from Mycobacterium tuberculosis (MtbRimMCTD) and the molecular mechanisms underlying MtbRimMCTD binding S19 remain elusive. Here, we report the solution structure, dynamics features of MtbRimMCTD, and its interaction with S19. MtbRimMCTD has a rigid hydrophobic core comprised of a relatively conservative six-strand β-barrel, tailed with a short α-helix and interspersed with flexible loops. Using several biophysical techniques including surface plasmon resonance (SPR) affinity assays, nuclear magnetic resonance (NMR) assays, and molecular docking, we established a structural model of the MtbRimMCTD–S19 complex and indicated that the β4-β5 loop and two nonconserved key residues (D105 and H129) significantly contributed to the unique pattern of MtbRimMCTD binding S19, which might be implicated in a form of orthogonality for species-dependent RimM–S19 interaction. Our study provides the structural basis for MtbRimMCTD binding S19 and is beneficial to the further exploration of MtbRimM as a potential target for the development of new anti-TB drugs.

Revisiting the NMR solution structure of the Cel48S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation

2014 ◽  
Vol 188 (2) ◽  
pp. 188-193 ◽  
Author(s):  
Chao Chen ◽  
Zhenling Cui ◽  
Yan Xiao ◽  
Qiu Cui ◽  
Steven P. Smith ◽  
...  
Keyword(s):  
Clostridium Thermocellum ◽  
Solution Structure ◽  
Type I ◽  
Nmr Solution Structure

scholarly journals Crystal Structure of the Ancient, Fe−S Scaffold IscA Reveals a Novel Protein Fold†

Biochemistry ◽  
2004 ◽  
Vol 43 (1) ◽  
pp. 133-139 ◽  
Author(s):  
Patrick W. Bilder ◽  
Huangen Ding ◽  
Marcia E. Newcomer
Keyword(s):  
Crystal Structure ◽  
Protein Fold ◽  
Novel Protein
Sign in / Sign up

Export Citation Format

Share Document