Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus Lon reveals the conformational variability in the active sites of Lon proteases

Journal of Molecular Biology

Volumn 351, Issue 1, 2005, Pages 144-157

  Botos, Istvan ^a   Melnikov, Edward E ^b   Cherry, Scott ^a   Kozlov, Serguei ^a   Makhovskaya, Oksana V ^b   Tropea, Joseph E ^a   Gustchina, Alla ^a   Rotanova, Tatyana V ^b   Wlodawer, Alexander ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Active site; Atomic resolution; ATP dependent proteases; Catalytic dyad; Structure comparisons

Indexed keywords

MUTANT PROTEIN; PROTEINASE; SOLVENT;

ARCHAEOGLOBUS FULGIDUS; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; GENETIC CONSERVATION; METHANOCOCCUS JANNASCHII; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN;

ARCHAEOGLOBUS FULGIDUS; METHANOCALDOCOCCUS JANNASCHII;

EID: 22044455121     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.06.008     Document Type: Article

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