The Active Site of a Lon Protease from Methanococcus jannaschii Distinctly Differs from the Canonical Catalytic Dyad of Lon Proteases

ATP-dependent Lon proteases catalyze the degradation of various regulatory proteins and abnormal proteins within cells. Methanococcus jannaschii Lon (Mj-Lon) is a homologue of Escherichia coli Lon (Ec-Lon) but has two transmembrane helices within its N-terminal ATPase domain. We solved the crystal s...

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Veröffentlicht in:	The Journal of biological chemistry 2004-12, Vol.279 (51), p.53451-53457
Hauptverfasser:	Im, Young Jun, Na, Young, Kang, Gil Bu, Rho, Seong-Hwan, Kim, Mun-Kyoung, Lee, Jun Hyuck, Chung, Chin Ha, Eom, Soo Hyun
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aspartic Acid - chemistry Binding Sites Catalysis Catalytic Domain Crystallography, X-Ray Escherichia coli Escherichia coli - enzymology Escherichia coli - metabolism Gene Library Hydrogen Bonding Hydrogen-Ion Concentration Lysine - chemistry Methanocaldococcus jannaschii Methanococcus - enzymology Models, Molecular Molecular Sequence Data Protease La - chemistry Protease La - classification Protease La - metabolism Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Serine - chemistry Serine Endopeptidases - chemistry Species Specificity Static Electricity Water - chemistry
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