The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.
Im
Young Jun
YJ
Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea.
Na
Young
Y
Kang
Gil Bu
GB
Rho
Seong-Hwan
SH
Kim
Mun-Kyoung
MK
Lee
Jun Hyuck
JH
Chung
Chin Ha
CH
Eom
Soo Hyun
SH
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
D014867:Water; D001224:Aspartic Acid; D012694:Serine; D012697:Serine Endopeptidases; D049070:Protease La; D008239:Lysine