Crystal Structure of 6α-(Hydroxymethyl)penicillanate Complexed to the TEM-1 β-Lactamase fromEscherichia coli:  Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided Process

1996 ◽  
Vol 118 (32) ◽  
pp. 7435-7440 ◽  
Author(s):  
Laurent Maveyraud ◽  
Irina Massova ◽  
Catherine Birck ◽  
Kazuyuki Miyashita ◽  
Jean-Pierre Samama ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mechanism Of Action ◽  
Fromescherichia Coli ◽  
Computer Aided

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 Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB fromEscherichia coli

2016 ◽  
Vol 25 (12) ◽  
pp. 2216-2224 ◽  
Author(s):  
Ekaterina V. Filippova ◽  
Zdzislaw Wawrzak ◽  
Jiapeng Ruan ◽  
Sergii Pshenychnyi ◽  
Richard M. Schultz ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Stress Response ◽  
Response Regulator ◽  
Fromescherichia Coli ◽  
Receiver Domain

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

scholarly journals Crystal structure of the thermostable mutant of hygromycin phosphotransferase fromEscherichia coli

2008 ◽  
Vol 64 (a1) ◽  
pp. C265-C265
Author(s):  
S. Yajima ◽  
D. Iino ◽  
Y. Sasaki ◽  
R. Kawakami ◽  
T. Hoshino ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Fromescherichia Coli ◽  
Hygromycin Phosphotransferase

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.

Computer-Aided Design of Compounds with Crystal Structure of Melilites

2020 ◽  
Vol 11 (4) ◽  
pp. 787-794
Author(s):  
N. N. Kiselyova ◽  
V. A. Dudarev ◽  
V. V. Ryazanov ◽  
O. V. Sen’ko ◽  
A. A. Dokukin
Keyword(s):  
Crystal Structure ◽  
Computer Aided Design ◽  
Computer Aided ◽  
Aided Design

The Crystal Structure of YdcE, a 4-Oxalocrotonate Tautomerase Homologue fromEscherichia coli, Confirms the Structural Basis for Oligomer Diversity†,‡

Biochemistry ◽  
2002 ◽  
Vol 41 (40) ◽  
pp. 12010-12024 ◽  
Author(s):  
Jeffrey J. Almrud ◽  
Andrew D. Kern ◽  
Susan C. Wang ◽  
Robert M. Czerwinski ◽  
William H. Johnson, ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structural Basis ◽  
Fromescherichia Coli

scholarly journals Crystal Structure of the Gephyrin-related Molybdenum Cofactor Biosynthesis Protein MogA fromEscherichia coli

2000 ◽  
Vol 275 (3) ◽  
pp. 1814-1822 ◽  
Author(s):  
Michael T. W. Liu ◽  
Margot M. Wuebbens ◽  
K. V. Rajagopalan ◽  
Hermann Schindelin
Keyword(s):  
Crystal Structure ◽  
Molybdenum Cofactor ◽  
Fromescherichia Coli ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis
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