Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 18, 2006, Pages 6829-6834

  Hänzelmann, Petra ^a   Schindelin, Hermann ^a,b  

^a STONY BROOK UNIVERSITY   (United States)

^b UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

GTP cyclohydrolase; Iron sulfur; Radicals molybdenum cofactor

Indexed keywords

CARBON; GUANINE; GUANOSINE; GUANOSINE TRIPHOSPHATE; HYDROGEN; IRON SULFUR PROTEIN; MOLYBDENUM; PROTEIN MOAA; PROTEIN MOAC; S ADENOSYLMETHIONINE; TETRAHYDROPYRANOPTERIN; UNCLASSIFIED DRUG; DRUG DERIVATIVE; HYDROLASE; METALLOPROTEIN; MOLYBDENUM COFACTOR; PTERIDINE DERIVATIVE; S ADENOSYLMETHIONINE ENZYME MOAA, STAPHYLOCOCCUS AUREUS; S-ADENOSYLMETHIONINE ENZYME MOAA, STAPHYLOCOCCUS AUREUS;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOSYNTHESIS; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME BINDING; PRIORITY JOURNAL; REACTION ANALYSIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COENZYME; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN CONFORMATION; STAPHYLOCOCCUS AUREUS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; COENZYMES; CRYSTALLOGRAPHY, X-RAY; GUANOSINE TRIPHOSPHATE; HYDROLASES; IRON-SULFUR PROTEINS; METALLOPROTEINS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; PTERIDINES; S-ADENOSYLMETHIONINE; STAPHYLOCOCCUS AUREUS;

EID: 33646468635     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0510711103     Document Type: Article

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