Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans

Structure

Volumn 24, Issue 8, 2016, Pages 1227-1236

  Hagmann, Anna ^a   Hunkeler, Moritz ^a   Stuttfeld, Edward ^a   Maier, Timm ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A CARBOXYLASE; BIOTIN; BIOTIN CARBOXYL CARRIER PROTEIN; BIOTIN CARBOXYLASE; CARBOXYL TRANSFERASE; CARBOXYLASE; DIMER; POLYPEPTIDE; UNCLASSIFIED DRUG; ACETYL COENZYME A CARBOXYLASE; BACTERIAL PROTEIN; FATTY ACID SYNTHASE; LIGASE; PROTEIN BINDING; RECOMBINANT PROTEIN; TRANSFERASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DEINOCOCCUS RADIODURANS; ELECTRON MICROSCOPY; ENZYME SPECIFICITY; ENZYME STRUCTURE; HISTOGRAM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; QUANTITATIVE ANALYSIS; RADIATION SCATTERING; SIZE EXCLUSION CHROMATOGRAPHY; SIZE EXCLUSION CHROMATOGRAPHY COUPLED WITH MULTI ANGLE LIGHT SCATTERING; X RAY CRYSTALLOGRAPHY; ALPHA HELIX; ANIMAL; BACULOVIRIDAE; BETA SHEET; BINDING SITE; CHEMISTRY; DEINOCOCCUS; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR MODEL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN MULTIMERIZATION; SF9 CELL LINE; SMALL ANGLE SCATTERING; SPODOPTERA; X RAY DIFFRACTION;

ACETYL-COA CARBOXYLASE; AMINO ACID MOTIFS; ANIMALS; BACTERIAL PROTEINS; BACULOVIRIDAE; BINDING SITES; BIOTIN; CARBON-NITROGEN LIGASES; CARBOXYL AND CARBAMOYL TRANSFERASES; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; DEINOCOCCUS; ESCHERICHIA COLI; FATTY ACID SYNTHASE, TYPE II; GENE EXPRESSION; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SCATTERING, SMALL ANGLE; SF9 CELLS; SPODOPTERA; SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

EID: 84979993893     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2016.06.001     Document Type: Article

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