On the significance of Toc-GTPase homodimers

Journal of Biological Chemistry

Volumn 283, Issue 34, 2008, Pages 23104-23112

  Koenig, Patrick ^a   Oreb, Mislav ^b   Rippe, Karsten ^c   Muhle Goll, Claudia ^d   Sinning, Irmgard ^a   Schleiff, Enrico ^b   Tews, Ivo ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b Department of Biosciences ^*  (Germany)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^d KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; CENTRIFUGATION; CHEMICAL ACTIVATION; CHLOROPHYLL; GALLIUM ALLOYS; NUCLEAR MAGNETIC RESONANCE; NUCLEIC ACIDS; NUCLEOTIDES; ORGANIC ACIDS;

ACTIVATING PROTEINS; ANALYTICAL ULTRACENTRIFUGATION; ARABIDOPSIS TOC33; CATALYTIC CENTERS; CHLOROPLAST MEMBRANES; CRYSTALLOGRAPHIC STRUCTURES; DIMERIC CONFORMATIONS; DO-MAINS; FUNCTIONAL MODELS; GTPASES; HOMODIMER; HOMODIMERIC SUBUNITS; HOMODIMERS; KINETIC STUDIES; NUCLEOTIDE BINDINGS; PRECURSOR PROTEINS; TRANSITION STATES;

AMINO ACIDS;

ALANINE; ARGININE; ENZYME VARIANT; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; HOMODIMER; MONOMER; PROTEIN TOC; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; TOC34 PROTEIN, PLANT; VEGETABLE PROTEIN;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ARTICLE; BINDING AFFINITY; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBUNIT; FLUORINE NUCLEAR MAGNETIC RESONANCE; MOLECULAR MODEL; PRIORITY JOURNAL; ULTRACENTRIFUGATION; WILD TYPE; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; BIOLOGICAL MODEL; BIOPHYSICS; CHEMISTRY; CONFORMATION; ENZYMOLOGY; METABOLISM; METHODOLOGY; MOLECULAR CLONING; MOLECULAR GENETICS; MUTATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

ARABIDOPSIS;

AMINO ACID SEQUENCE; ARABIDOPSIS; BIOPHYSICS; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GTP PHOSPHOHYDROLASES; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MUTATION; PLANT PROTEINS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 53149117483     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M710576200     Document Type: Article

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