Crucial roles of single residues in binding affinity, specificity, and promiscuity in the cellulosomal cohesin-dockerin interface

Journal of Biological Chemistry

Volumn 290, Issue 22, 2015, Pages 13654-13666

  Slutzki, Michal ^a   Reshef, Dan ^b   Barak, Yoav ^a   Haimovitz, Rachel ^a   Rotem Bamberger, Shahar ^b   Lamed, Raphael ^c   Bayer, Edward A ^a   Schueler Furman, Ora ^b  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b HEBREW UNIVERSITY   (Israel)

^c TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CLOSTRIDIUM;

BINDING AFFINITIES; BINDING SPECIFICITIES; CLOSTRIDIUM CELLULOLYTICUM; CLOSTRIDIUM THERMOCELLUM; COMPUTATIONAL DESIGN; EVOLUTIONARY DYNAMICS; SINGLE MUTATION; SINGLE RESIDUE;

BINS;

CELLULOSOME; COHESIN; DOCKERIN; MEMBRANE ENZYME; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARBOHYDRATE; CARRIER PROTEIN; CELL CYCLE PROTEIN; CELLULOSE; NONHISTONE PROTEIN; PROTEIN BINDING;

ARTICLE; BINDING AFFINITY; CLOSTRIDIUM CELLULOLYTICUM; CLOSTRIDIUM THERMOCELLUM; COMPUTER SIMULATION; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; BIOLOGY; CHEMISTRY; COMPUTER PROGRAM; IC50; METABOLISM; MUTATION; PROTEIN MICROARRAY; PROTEIN TERTIARY STRUCTURE; SPECIES DIFFERENCE; THERMODYNAMICS;

CLOSTRIDIUM CELLULOLYTICUM; CLOSTRIDIUM THERMOCELLUM;

BACTERIAL PROTEINS; CARBOHYDRATES; CARRIER PROTEINS; CELL CYCLE PROTEINS; CELLULOSE; CHROMOSOMAL PROTEINS, NON-HISTONE; CLOSTRIDIUM CELLULOLYTICUM; CLOSTRIDIUM THERMOCELLUM; COMPUTATIONAL BIOLOGY; ENZYME-LINKED IMMUNOSORBENT ASSAY; INHIBITORY CONCENTRATION 50; MUTATION; PROTEIN ARRAY ANALYSIS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SOFTWARE; SPECIES SPECIFICITY; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 84930684278     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.651208     Document Type: Article

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