The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

Structure

Volumn 3, Issue 11, 1995, Pages 1147-1158

  Yip, KSP ^a   Stillman, TJ ^a   Britton, KL ^a   Artymiuk, PJ ^a   Baker, PJ ^a   Sedelnikova, SE ^a   Engel, PC ^a   Pasquo, A ^b   Chiaraluce, R ^b   Consalvi, V ^b   Scandurra, R ^b   Rice, DW ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

glutamate dehydrogenase; hyperthermophile; Pyrococcus furiosus; thermal stability; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; GLUTAMATE DEHYDROGENASE; ION;

AMINO ACID SEQUENCE; ARCHAEBACTERIUM; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; HYDROGEN BOND; MOLECULAR GENETICS; PHYSICAL CHEMISTRY; PROTEIN CONFORMATION; PROTEIN DENATURATION; SEQUENCE ALIGNMENT; TEMPERATURE;

AMINO ACID SEQUENCE; ARCHAEA; BACTERIAL PROTEINS; CHEMISTRY, PHYSICAL; GLUTAMATE DEHYDROGENASE; HYDROGEN BONDING; IONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN DENATURATION; SEQUENCE ALIGNMENT; TEMPERATURE;

ARCHAEA; BACTERIA (MICROORGANISMS); PYROCOCCUS FURIOSUS;

EID: 13244249836     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00251-9     Document Type: Article

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