Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism

Acta Crystallographica Section D: Biological Crystallography

Volumn 68, Issue 11, 2012, Pages 1488-1500

  Lee, Byung Gil ^a   Kim, Min Kyung ^a   Kim, Byeong Won ^a   Suh, Se Won ^b   Song, Hyun Kyu ^a  

^a Korea University   (South Korea)

^b Seoul National University   (South Korea)

Author keywords

barley; cereal crops; monocots; RIP; surface entropy reduction

Indexed keywords

ADENINE; ADENOSINE PHOSPHATE; HYBRID PROTEIN; RIBOSOME INACTIVATING PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; HORDEUM; METABOLISM; MOLECULAR GENETICS; PLANT SEED; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; UPREGULATION; X RAY CRYSTALLOGRAPHY;

ADENINE; ADENOSINE MONOPHOSPHATE; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ESCHERICHIA COLI; HORDEUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; RIBOSOME INACTIVATING PROTEINS; SEEDS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN; UP-REGULATION;

EID: 84867787918     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444912037110     Document Type: Article

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