scholarly journals The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitors

2014 ◽  
Vol 23 (6) ◽  
pp. 723-734 ◽  
Author(s):  
Sebastian M. Lambert ◽  
David R. Langley ◽  
James A. Garnett ◽  
Richard Angell ◽  
Katy Hedgethorne ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mechanism Of Action ◽  
Genotype 1A

Crystal Structure of HIV-1 Reverse Transcriptase Bound to a Non-Nucleoside Inhibitor with a Novel Mechanism of Action

2010 ◽  
Vol 122 (10) ◽  
pp. 1849-1852 ◽  
Author(s):  
Séverine Freisz ◽  
Guillaume Bec ◽  
Marco Radi ◽  
Philippe Wolff ◽  
Emmanuele Crespan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Reverse Transcriptase ◽  
Mechanism Of Action ◽  
Hiv 1

scholarly journals Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase

2002 ◽  
Vol 99 (4) ◽  
pp. 1859-1864 ◽  
Author(s):  
J. A. R. G. Barbosa ◽  
J. Sivaraman ◽  
Y. Li ◽  
R. Larocque ◽  
A. Matte ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mechanism Of Action ◽  
Binding Mode ◽  
Histidinol Dehydrogenase

scholarly journals Structural analysis of a novel substrate-free form of the aminoglycoside 6′-N-acetyltransferase from Enterococcus faecium

2020 ◽  
Vol 76 (8) ◽  
pp. 364-371
Author(s):  
Hyunseok Jang ◽  
Sunghark Kwon ◽  
Chang-Sook Jeong ◽  
Chang Woo Lee ◽  
Jisub Hwang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Mechanism Of Action ◽  
Enterococcus Faecium ◽  
Free Form ◽  
Amino Group ◽  
Detailed Mechanism ◽  
Conformational Selection ◽  
Enzymatic Function ◽  
Acetyl Group

Aminoglycoside acetyltransferases (AACs) catalyze the transfer of an acetyl group between acetyl-CoA and an aminoglycoside, producing CoA and an acetylated aminoglycoside. AAC(6′)-Ii enzymes target the amino group linked to the 6′ C atom in an aminoglycoside. Several structures of the AAC(6′)-Ii from Enterococcus faecium [Ef-AAC(6′)-Ii] have been reported to date. However, the detailed mechanism of its enzymatic function remains elusive. In this study, the crystal structure of Ef-AAC(6′)-Ii was determined in a novel substrate-free form. Based on structural analysis, it is proposed that Ef-AAC(6′)-Ii sequentially undergoes conformational selection and induced fit for substrate binding. These results therefore provide a novel viewpoint on the mechanism of action of Ef-AAC(6′)-Ii.

scholarly journals Synthesis, Crystal Structure, Cytotoxicity, and Mechanism of Action of ZnII, MnII, and FeIIIComplexes with 6-Hydroxyloxoisoaporphine

2017 ◽  
Vol 2017 (12) ◽  
pp. 1824-1834 ◽  
Author(s):  
Qi-Pin Qin ◽  
Ting Meng ◽  
Zu-Zhuang Wei ◽  
Chuan-Hui Zhang ◽  
Yan-Cheng Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mechanism Of Action

scholarly journals Three novel transition metal complexes of 6-methyl-2-oxo-quinoline-3-carbaldehyde thiosemicarbazone: synthesis, crystal structure, cytotoxicity, and mechanism of action

RSC Advances ◽  
2017 ◽  
Vol 7 (29) ◽  
pp. 17923-17933 ◽  
Author(s):  
Bi-Qun Zou ◽  
Xing Lu ◽  
Qi-Pin Qin ◽  
Yu-Xia Bai ◽  
Ye Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Transition Metal ◽  
Metal Complexes ◽  
Mitochondrial Dysfunction ◽  
Tumor Cells ◽  
Transition Metal Complexes ◽  
Mechanism Of Action ◽  
Normal Cells

Complex 1 was more selective for MGC80-3 tumor cells versus normal cells (HL-7702). Importantly, 1 triggered MGC80-3 cells apoptosis via a mitochondrial dysfunction pathway.

scholarly journals Crystal structure of a β-aminopeptidase from an AustralianBurkholderiasp.

2017 ◽  
Vol 73 (7) ◽  
pp. 386-392 ◽  
Author(s):  
Marietta John-White ◽  
Geoff J. Dumsday ◽  
Priscilla Johanesen ◽  
Dena Lyras ◽  
Nyssa Drinkwater ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Wastewater Treatment ◽  
Mechanism Of Action ◽  
Treatment Plant ◽  
Β Subunit ◽  
Α Subunit ◽  
Gram Negative ◽  
X Ray ◽  
Tetrameric Assembly

β-Aminopeptidases are a unique group of enzymes that have the unusual capability to hydrolyze N-terminal β-amino acids from synthetic β-peptides. β-Peptides can form secondary structures mimicking α-peptide-like structures that are resistant to degradation by most known proteases and peptidases. These characteristics of β-peptides give them great potential as peptidomimetics. Here, the X-ray crystal structure of BcA5-BapA, a β-aminopeptidase from a Gram-negativeBurkholderiasp. that was isolated from activated sludge from a wastewater-treatment plant in Australia, is reported. The crystal structure of BcA5-BapA was determined to a resolution of 2.0 Å and showed a tetrameric assembly typical of the β-aminopeptidases. Each monomer consists of an α-subunit (residues 1–238) and a β-subunit (residues 239–367). Comparison of the structure of BcA5-BapA with those of other known β-aminopeptidases shows a highly conserved structure and suggests a similar proteolytic mechanism of action.

Two pore residues mediate acidosis-induced enhancement of C-type inactivation of the Kv1.4 K+ channel

2002 ◽  
Vol 283 (4) ◽  
pp. C1114-C1121 ◽  
Author(s):  
T. W. Claydon ◽  
M. R. Boyett ◽  
A. Sivaprasadarao ◽  
C. H. Orchard
Keyword(s):  
Crystal Structure ◽  
Voltage Clamp ◽  
Mechanism Of Action ◽  
Xenopus Oocytes ◽  
K Channel ◽  
Positively Charged

Acidosis inhibits current through the Kv1.4 K+ channel, perhaps as a result of enhancement of C-type inactivation. The mechanism of action of acidosis on C-type inactivation has been studied. A mutant Kv1.4 channel that lacks N-type inactivation (fKv1.4 Δ2–146) was expressed in Xenopus oocytes, and currents were recorded using two-microelectrode voltage clamp. Acidosis increased fKv1.4 Δ2–146 C-type inactivation. Replacement of a pore histidine with cysteine (H508C) abolished the increase. Application of positively charged thiol-specific methanethiosulfonate to fKv1.4 Δ2–146 H508C increased C-type inactivation, mimicking the effect of acidosis. Replacement of a pore lysine with cysteine (K532C) abolished the acidosis-induced increase of C-type inactivation. A model of the Kv1.4 pore, based on the crystal structure of KcsA, shows that H508 and K532 lie close together. It is suggested that the acidosis-induced increase of C-type inactivation involves the charge on H508 and K532.

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