title: The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.
authors.affiliation: Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea.
authors.forename: Young Jun
authors.initials: YJ
authors.lastname: Im
authors.forename: Young
authors.initials: Y
authors.lastname: Na
authors.forename: Gil Bu
authors.initials: GB
authors.lastname: Kang
authors.forename: Seong-Hwan
authors.initials: SH
authors.lastname: Rho
authors.forename: Mun-Kyoung
authors.initials: MK
authors.lastname: Kim
authors.forename: Jun Hyuck
authors.initials: JH
authors.lastname: Lee
authors.forename: Chin Ha
authors.initials: CH
authors.lastname: Chung
authors.forename: Soo Hyun
authors.initials: SH
authors.lastname: Eom
mesh_terms: D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000737:chemistry; D001665:Binding Sites; D002384:Catalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D015723:Gene Library; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D008239:Lysine / Q000737:chemistry; D017017:Methanococcus / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D049070:Protease La / Q000737:chemistry* / Q000145:classification* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry; D013045:Species Specificity; D055672:Static Electricity; D014867:Water / Q000737:chemistry
chemical_list: D014867:Water; D001224:Aspartic Acid; D012694:Serine; D012697:Serine Endopeptidases; D049070:Protease La; D008239:Lysine