Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from staphylococcus aureus

1998 ◽  
Vol 5 (5) ◽  
pp. 357-362 ◽  
Author(s):  
Michael Hennig ◽  
Allan D′Arcy ◽  
Isabella C. Hampele ◽  
Malcolm G.P. Page ◽  
Christian Oefner ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Reaction Mechanism ◽  
Dihydroneopterin Aldolase

scholarly journals Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus

2018 ◽  
Vol 74 (10) ◽  
pp. 632-637
Author(s):  
Lisha Ha ◽  
Jennifer Colquhoun ◽  
Nicholas Noinaj ◽  
Chittaranjan Das ◽  
Paul M. Dunman ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Rna Processing ◽  
Bacterial Species ◽  
Rna Degradation ◽  
Ribonuclease P ◽  
Protein Subunit ◽  
Aromatic Residues ◽  
Cellular Processes ◽  
P Protein

Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein component for two essential cellular processes, RNA degradation and transfer-RNA (tRNA) maturation. The first crystal structure of RnpA from the pathogenic bacterial species, S. aureus, is reported at 2.0 Å resolution. The structure presented maintains key similarities with previously reported RnpA structures from bacteria and archaea, including the highly conserved RNR-box region and aromatic residues in the precursor-tRNA 5′-leader-binding domain. This structure will be instrumental in the pursuit of structure-based designed inhibitors targeting RnpA-mediated RNA processing as a novel therapeutic approach for treating S. aureus infections.

The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities

2014 ◽  
Vol 70 (12) ◽  
pp. 3212-3225 ◽  
Author(s):  
Tiila-Riikka Kiema ◽  
Rajesh K. Harijan ◽  
Malgorzata Strozyk ◽  
Toshiyuki Fukao ◽  
Stefan E. H. Alexson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Reaction Mechanism ◽  
Active Site ◽  
Quaternary Structure ◽  
Fatty Acyl ◽  
Physiological Importance ◽  
Loop Domain ◽  
Solution Studies ◽  
Hydrolysis Of ◽  
Insight Into

Crystal structures of human mitochondrial 3-ketoacyl-CoA thiolase (hT1) in the apo form and in complex with CoA have been determined at 2.0 Å resolution. The structures confirm the tetrameric quaternary structure of this degradative thiolase. The active site is surprisingly similar to the active site of theZoogloea ramigerabiosynthetic tetrameric thiolase (PDB entries 1dm3 and 1m1o) and different from the active site of the peroxisomal dimeric degradative thiolase (PDB entries 1afw and 2iik). A cavity analysis suggests a mode of binding for the fatty-acyl tail in a tunnel lined by the Nβ2–Nα2 loop of the adjacent subunit and the Lα1 helix of the loop domain. Soaking of the apo hT1 crystals with octanoyl-CoA resulted in a crystal structure in complex with CoA owing to the intrinsic acyl-CoA thioesterase activity of hT1. Solution studies confirm that hT1 has low acyl-CoA thioesterase activity for fatty acyl-CoA substrates. The fastest rate is observed for the hydrolysis of butyryl-CoA. It is also shown that T1 has significant biosynthetic thiolase activity, which is predicted to be of physiological importance.

scholarly journals Crystal Structure of SANOS, a Bacterial Nitric Oxide Synthase Oxygenase Protein from Staphylococcus aureus

Structure ◽  
2002 ◽  
Vol 10 (12) ◽  
pp. 1687-1696 ◽  
Author(s):  
Louise E Bird ◽  
Jingshan Ren ◽  
Jiancheng Zhang ◽  
Neale Foxwell ◽  
Alastair R Hawkins ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitric Oxide ◽  
Staphylococcus Aureus ◽  
Nitric Oxide Synthase ◽  
Oxide Synthase

Preparation, Characterisation, Crystal Structure and Antibacterial Activity of two Bis-Schiff Bases Containing a Piperazine Ring

2018 ◽  
Vol 42 (10) ◽  
pp. 512-514
Author(s):  
Rui-bo Xu ◽  
Xiao-tian Yang ◽  
Hai-nan Li ◽  
Peng-cheng Zhao ◽  
Jiao-jiao Li ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Bacillus Subtilis ◽  
Schiff Bases ◽  
Piperazine Ring ◽  
X Ray ◽  
X Ray Crystallography ◽  
Good Antibacterial Activity

Two new bis-Schiff bases containing a piperazine ring, N,N‘-bis(4-chlorobenzylidene)- and N,N‘-bis(4-cyanobenzylidene)-1,4-bis(3-aminopropyl)piperazine, were prepared by the reaction of N,N‘-bis(3-aminopropyl)piperazine with 4-chloro- and 4-cyanobenzaldehyde, respectively. The dichloro compound was fully identified by X-ray crystallography and it exhibited good antibacterial activity against Escherichia coli, Staphylococcus aureus and Bacillus subtilis.

scholarly journals Crystal structure of the yeast His6 enzyme suggests a reaction mechanism

2006 ◽  
Vol 15 (6) ◽  
pp. 1516-1521 ◽  
Author(s):  
Sophie Quevillon-Cheruel ◽  
Nicolas Leulliot ◽  
Marc Graille ◽  
Karine Blondeau ◽  
Joel Janin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Reaction Mechanism

Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family

2017 ◽  
Vol 36 (2) ◽  
pp. 376-386 ◽  
Author(s):  
Yuri N. Chirgadze ◽  
Eugenia A. Boshkova ◽  
Kevin P. Battaile ◽  
Vitor G. Mendes ◽  
Robert Lam ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Glyoxalase I

Crystal structure and activities of three biscoumarin derivatives against Staphylococcus aureus

2015 ◽  
Vol 1097 ◽  
pp. 117-123 ◽  
Author(s):  
Fen Li ◽  
Chang-wei Lv ◽  
Zi-dan Zhang ◽  
Jing Li ◽  
Zheng Hou ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus
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