Structures of Thermophilic and Mesophilic Adenylate Kinases from the Genus Methanococcus

The crystal structures of adenylate kinases from the thermophile Methanococcus thermolithotrophicus and the mesophile Methanococcus voltae have been solved to resolutions of 2.8 Å and 2.5 Å, respectively. The structures of the enzymes are similar to that of the adenylate kinase from archaeal Sulfolo...

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Veröffentlicht in:	Journal of molecular biology 2003-07, Vol.330 (5), p.1087-1099
Hauptverfasser:	Criswell, Angela R., Bae, Euiyoung, Stec, Boguslaw, Konisky, Jordan, Phillips Jr, George N.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Monophosphate - chemistry adenylate kinase Adenylate Kinase - chemistry Amino Acid Sequence Arginine - chemistry Binding Sites Crystallography, X-Ray DNA Mutational Analysis Escherichia coli - metabolism Hydrogen Bonding Ligands Lysine - chemistry Methanococcus Methanococcus - enzymology Methanococcus thermolithotrophicus Methanococcus voltae Models, Chemical Models, Molecular Molecular Sequence Data phosphate-binding loop Plasmids - metabolism Protein Binding Protein Conformation Protein Structure, Tertiary protein thermostability Sequence Homology, Amino Acid Temperature X-ray crystallography
Online-Zugang:	Volltext
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