Structural basis of tRNA discrimination as derived from the high resolution crystal structure of glutaminyl-tRNA synthetase complexed with tRNAGln and ATP

1990 ◽  
Vol 14 (2-3) ◽  
pp. 213-214 ◽  
Author(s):  
T. A. Steitz ◽  
M. A. Rould ◽  
J. J. Perona
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Trna Synthetase ◽  
Structural Basis

scholarly journals High resolution crystal structure of PedB: a structural basis for the classification of pediocin-like immunity proteins

2007 ◽  
Vol 7 (1) ◽  
pp. 35 ◽  
Author(s):  
In-Kwon Kim ◽  
Min-Kyu Kim ◽  
Ji-Hye Kim ◽  
Hyung-Soon Yim ◽  
Sun-Shin Cha ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Structural Basis

The high-resolution crystal structure of phosphatidylinositol 4-kinase IIβ and the crystal structure of phosphatidylinositol 4-kinase IIα containing a nucleoside analogue provide a structural basis for isoform-specific inhibitor design

2015 ◽  
Vol 71 (7) ◽  
pp. 1555-1563 ◽  
Author(s):  
Martin Klima ◽  
Adriana Baumlova ◽  
Dominika Chalupska ◽  
Hubert Hřebabecký ◽  
Milan Dejmek ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Nucleoside Analogue ◽  
Specific Inhibitor ◽  
Eukaryotic Cells ◽  
Structural Basis ◽  
Conformational Heterogeneity ◽  
Inhibitor Design ◽  
Hydrophobic Pocket ◽  
Phosphatidylinositol 4

Phosphatidylinositol 4-phosphate (PI4P) is the most abundant monophosphoinositide in eukaryotic cells. Humans have four phosphatidylinositol 4-kinases (PI4Ks) that synthesize PI4P, among which are PI4K IIβ and PI4K IIα. In this study, two crystal structures are presented: the structure of human PI4K IIβ and the structure of PI4K IIα containing a nucleoside analogue. The former, a complex with ATP, is the first high-resolution (1.9 Å) structure of a PI4K. These structures reveal new details such as high conformational heterogeneity of the lateral hydrophobic pocket of the C-lobe and together provide a structural basis for isoform-specific inhibitor design.

scholarly journals Correction: High Resolution Crystal Structure of Human β-Glucuronidase Reveals Structural Basis of Lysosome Targeting

PLoS ONE ◽  
2015 ◽  
Vol 10 (9) ◽  
pp. e0138401 ◽  
Author(s):  
Md. Imtaiyaz Hassan ◽  
Abdul Waheed ◽  
Jeffery H. Grubb ◽  
Herbert E. Klei ◽  
Sergey Korolev ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Structural Basis

scholarly journals Structural basis for ion selectivity revealed by high-resolution crystal structure of Mg2+ channel MgtE

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Hironori Takeda ◽  
Motoyuki Hattori ◽  
Tomohiro Nishizawa ◽  
Keitaro Yamashita ◽  
Syed T. A. Shah ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Ion Selectivity ◽  
Structural Basis

scholarly journals High Resolution Crystal Structure of Human β-Glucuronidase Reveals Structural Basis of Lysosome Targeting

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e79687 ◽  
Author(s):  
Md. Imtaiyaz Hassan ◽  
Abdul Waheed ◽  
Jeffery H. Grubb ◽  
Herbert E. Klei ◽  
Sergey Korolev ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Structural Basis

scholarly journals Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Manmohan Sharma ◽  
Nipun Malhotra ◽  
Manickam Yogavel ◽  
Karl Harlos ◽  
Bruno Melillo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Synthesis ◽  
Single Dose ◽  
Molecular Basis ◽  
Malaria Parasite ◽  
Trna Synthetase ◽  
Structural Basis ◽  
Atp Binding Site ◽  
Structural Framework ◽  
Competitive Inhibitors

AbstractThe inhibition of Plasmodium cytosolic phenylalanine tRNA-synthetase (cFRS) by a novel series of bicyclic azetidines has shown the potential to prevent malaria transmission, provide prophylaxis, and offer single-dose cure in animal models of malaria. To date, however, the molecular basis of Plasmodium cFRS inhibition by bicyclic azetidines has remained unknown. Here, we present structural and biochemical evidence that bicyclic azetidines are competitive inhibitors of L-Phe, one of three substrates required for the cFRS-catalyzed aminoacylation reaction that underpins protein synthesis in the parasite. Critically, our co-crystal structure of a PvcFRS-BRD1389 complex shows that the bicyclic azetidine ligand binds to two distinct sub-sites within the PvcFRS catalytic site. The ligand occupies the L-Phe site along with an auxiliary cavity and traverses past the ATP binding site. Given that BRD1389 recognition residues are conserved amongst apicomplexan FRSs, this work lays a structural framework for the development of drugs against both Plasmodium and related apicomplexans.

High resolution STEM imaging study on high Tc superconductor YBa2CuaO7-x

1988 ◽  
Vol 46 ◽  
pp. 882-883
Author(s):  
H.-J. Ou ◽  
J. M. Cowley
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Grain Boundary ◽  
Strong Field ◽  
Imaging Study ◽  
Structure Defects ◽  
High Tc ◽  
High Tc Superconductor ◽  
Diffraction Patterns ◽  
Lattice Planes

Using the dedicate VG-HB5 STEM microscope, the crystal structure of high Tc superconductor of YBa2Cu3O7-x has been studied via high resolution STEM (HRSTEM) imaging and nanobeam (∽3A) diffraction patterns. Figure 1(a) and 2(a) illustrate the HRSTEM image taken at 10' times magnification along [001] direction and [100] direction, respectively. In figure 1(a), a grain boundary with strong field contrast is seen between two crystal regions A and B. The grain boundary appears to be parallel to a (110) plane, although it is not possible to determine [100] and [001] axes as it is in other regions which contain twin planes [3]. Following the horizontal lattice lines, from left to right across the grain boundary, a lattice bending of ∽4° is noticed. Three extra lattice planes, indicated by arrows, were found to terminate at the grain boundary and form dislocations. It is believed that due to different chemical composition, such structure defects occur during crystal growth. No bending is observed along the vertical lattice lines.

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

Perovskite Solar Cells: Crystal Structure and Interface Architecture with High Resolution TEM Observations

2017 ◽  
Author(s):  
Satoshi Uchida ◽  
Tae Woong Kim ◽  
Ludmila Cojocaru ◽  
Takashi Kondo ◽  
Hiroshi Segawa
Keyword(s):  
Crystal Structure ◽  
Solar Cells ◽  
High Resolution ◽  
Perovskite Solar Cells ◽  
High Resolution Tem
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