Synthesis, crystal structure and action on Escherichia coli by microcalorimetry of copper complexes with 1,10-phenanthroline and amino acid

2011 ◽  
Vol 105 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Xi Li ◽  
Zhijun Zhang ◽  
Chenggang Wang ◽  
Tian Zhang ◽  
Kang He ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Amino Acid ◽  
Copper Complexes

Studies on Antibacterial Mechanisms of Copper Complexes with 1,10-phenanthroline and Amino Acid on Escherichia coli

2013 ◽  
Vol 154 (1) ◽  
pp. 150-155 ◽  
Author(s):  
Xin Liu ◽  
Xi Li ◽  
Zhijun Zhang ◽  
Yulin Dong ◽  
Peng Liu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Copper Complexes

scholarly journals A Novel Two-domain Architecture Within the Amino Acid Kinase Enzyme Family Revealed by the Crystal Structure of Escherichia coli Glutamate 5-kinase

2007 ◽  
Vol 367 (5) ◽  
pp. 1431-1446 ◽  
Author(s):  
Clara Marco-Marín ◽  
Fernando Gil-Ortiz ◽  
Isabel Pérez-Arellano ◽  
Javier Cervera ◽  
Ignacio Fita ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Amino Acid ◽  
Domain Architecture ◽  
Enzyme Family

Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase

1999 ◽  
Vol 55 (8) ◽  
pp. 1474-1477 ◽  
Author(s):  
Tzu-Ping Ko ◽  
Szu-Pei Wu ◽  
Wei-Zen Yang ◽  
Hsin Tsai ◽  
Hanna S. Yuan
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Covalent Bond ◽  
Tyrosine Aminotransferase ◽  
Crystallographic Analysis ◽  
Molecular Replacement ◽  
E Coli ◽  
Open Conformation

Tyrosine aminotransferase catalyzes transamination for both dicarboxylic and aromatic amino-acid substrates. The substrate-free Escherichia coli tyrosine aminotransferase (eTAT) bound with the cofactor pyridoxal 5′-phosphate (PLP) was crystallized in the trigonal space group P32. A low-resolution crystal structure of eTAT was determined by molecular-replacement methods. The overall folding of eTAT resembles that of the aspartate aminotransferases, with the two identical subunits forming a dimer in which each monomer binds a PLP molecule via a covalent bond linked to the ∊-NH2 group of Lys258. Comparison of the structure of eTAT with those of the open, half-open or closed form of chicken or E. coli aspartate aminotransferases shows the eTAT structure to be in the open conformation.

Crystal Structure of Murein-Tripeptide Amidase MpaA from Escherichia coli O157 at 2.6 Å Resolution

2017 ◽  
Vol 24 (2) ◽  
pp. 181-187 ◽  
Author(s):  
Yinliang Ma ◽  
Guohui Bai ◽  
Yaqi Cui ◽  
Jing Zhao ◽  
Zenglin Yuan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Escherichia Coli O157
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