Connected cavity structure enables prenyl elongation across the dimer interface in mutated geranylfarnesyl diphosphate synthase from Methanosarcina mazei

Biochemical and Biophysical Research Communications

Volumn 409, Issue 2, 2011, Pages 333-337

  Ogawa, Takuya ^a   Yoshimura, Tohru ^a   Hemmi, Hisashi ^a  

^a NAGOYA UNIVERSITY   (Japan)

Author keywords

Archaea; Geranylfarnesyl diphosphate synthase; Homology modeling; Isoprenoid; Mutagenesis; Prenyltransferase

Indexed keywords

DIMER; DIMETHYLALLYLTRANSFERASE; GERANYLFARNESYL DIPHOSPHATE SYNTHASE; ISOLEUCINE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CELL ELONGATION; ENZYME ACTIVITY; METHANOSARCINA MAZEI; MOLECULAR MECHANICS; MUTANT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; GERANYLTRANSTRANSFERASE; ISOLEUCINE; METHANOSARCINA; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY;

ARCHAEA; METHANOSARCINA MAZEI;

EID: 79957897289     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.05.018     Document Type: Article

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