Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism

Journal of Biological Chemistry

Volumn 288, Issue 50, 2013, Pages 35801-35811

  Murray, David S ^a   Chinnam, Nagababu ^b   Tonthat, Nam Ky ^b   Whitfill, Travis ^b   Wray Jr , Lewis V ^c   Fisher, Susan H ^c   Schumacher, Maria A ^b  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

^c BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; ENZYME ACTIVE SITES; FEEDBACK INHIBITION; GLUTAMINE SYNTHETASE; GRAM-POSITIVE PATHOGENS; HYDROGEN BOND NETWORKS; NITROGEN METABOLISM; REGULATORY MECHANISM;

AMINO ACIDS; CATALYSIS; HYDROGEN BONDS; ISOENZYMES;

ENZYME INHIBITION;

ALANINE; ARGININE; GLUTAMATE AMMONIA LIGASE; GLUTAMINE; GLUTAMINE SYNTHETASE ISOENZYME ALPHA; HYDROGEN; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROGEN BOND; IN VIVO STUDY; MUTATION; NONHUMAN; PRIORITY JOURNAL;

COOPERATIVITY; ENZYME CATALYSIS; ENZYME INACTIVATION; ENZYME MECHANISMS; ENZYME STRUCTURE; GLUTAMINE;

BACILLUS SUBTILIS; BIOCATALYSIS; FEEDBACK, PHYSIOLOGICAL; GLUTAMATE-AMMONIA LIGASE; GLUTAMINE; ISOENZYMES; KINETICS; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS;

EID: 84890327100     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.519496     Document Type: Article

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