The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability

Journal of Molecular Biology

Volumn 297, Issue 3, 2000, Pages 659-672

  Dams, Thomas ^a,b   Auerbach, Günter ^b   Bader, Gerd ^b   Jacob, Uwe ^b   Ploom, Tarmo ^b   Huber, Robert ^b   Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Conformational flexibility; Dihydrofolate reductase; Dimerization; Thermostability; Thermotoga

Indexed keywords

DIHYDROFOLATE REDUCTASE; DIMER; METHOTREXATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL; PROTEIN POLYMERIZATION; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; THERMOSTABILITY; THERMOTOGA MARITIMA;

BACTERIA (MICROORGANISMS); THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0034737320     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3570     Document Type: Article

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