Structural and Functional Characterization of an Ancient Bacterial Transglutaminase Sheds Light on the Minimal Requirements for Protein Cross-Linking

Biochemistry

Volumn 54, Issue 37, 2015, Pages 5723-5734

  Fernandes, Catarina G ^a,c   Plácido, Diana ^a   Lousa, Diana ^a   Brito, José A ^a   Isidro, Anabela ^a,d   Soares, Cláudio M ^a   Pohl, Jan ^b   Carrondo, Maria A ^a   Archer, Margarida ^a   Henriques, Adriano O ^a  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b CENTERS FOR DISEASE CONTROL AND PREVENTION   (United States)

^c EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d Portuguese Science and Technology Foundation   (Portugal)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BACTERIOLOGY; CELL MEMBRANES; CROSSLINKING; CRYSTAL STRUCTURE; PLANTS (BOTANY); PROTEINS;

BACILLUS SUBTILIS; CELLULAR STRUCTURE; FUNCTIONAL CHARACTERIZATION; HYDROPHOBIC TUNNEL; PROTEIN CROSSLINKING; SINGLE-DOMAIN PROTEINS; SPORE-FORMING BACTERIA; TRANSGLUTAMINASES;

HYDROGELS;

AMINO ACID; CYSTEINE PROTEINASE; MERCAPTAMINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEINASE; BACTERIAL PROTEIN; CROSS LINKING REAGENT;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; BACILLUS SUBTILIS; BACTERIAL CELL WALL; CATALYSIS; CELL WALL; CLOSTRIDIUM; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; CRYSTALLIZATION; ELECTRON; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NONHUMAN; PH; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN FOLDING; SPOROGENESIS; STRUCTURE ACTIVITY RELATION; CHEMICAL PHENOMENA; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CROSS-LINKING REAGENTS; CRYSTALLOGRAPHY, X-RAY; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR DYNAMICS SIMULATION; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; TRANSGLUTAMINASES;

EID: 84942100927     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00661     Document Type: Article

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