Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain

Journal of Biological Chemistry

Volumn 289, Issue 24, 2014, Pages 16855-16865

  Yokom, Adam L ^a,b   Morishima, Yoshihiro ^a   Lau, Miranda ^a   Su, Min ^b   Glukhova, Alisa ^b   Osawa, Yoichi ^a   Southworth, Daniel R ^a,b  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BLOOD PRESSURE; CALMODULIN; CAMS; DIMERS; ELECTRON TRANSITIONS;

CONFORMATIONAL CHANGE; CONFORMATIONAL STATE; ELECTRON TRANSFER MECHANISMS; ELECTRON-TRANSFER STEP; NITRIC-OXIDE SYNTHASE; STRUCTURAL ARRANGEMENT; STRUCTURAL MECHANISMS; THREE-DIMENSIONAL RECONSTRUCTION;

CONFORMATIONS;

CALMODULIN; DIMER; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; HEME; HOLOENZYME; INTERFLAVIN; NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE; OXYGENASE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME CONFORMATION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION; THREE DIMENSIONAL IMAGING;

CALMODULIN; ELECTRON MICROSCOPY (EM); FLAVOPROTEINS; NITRIC-OXIDE SYNTHASE; OXIDATION-REDUCTION;

AMINO ACID SEQUENCE; ANIMALS; CALMODULIN; CATALYTIC DOMAIN; HOLOENZYMES; MOLECULAR SEQUENCE DATA; NITRIC OXIDE SYNTHASE TYPE I; PROTEIN BINDING; RATS;

EID: 84902438336     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.564005     Document Type: Article

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