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Quaternary organization of subunits in the L‐leucine dehydrogenase from Bacillus cereus
Author(s) -
Lünsdorf Heinrich,
Tsai Hsin
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80165-4
Subject(s) - protein quaternary structure , bacillus cereus , electron microscope , protein subunit , crystallography , monomer , diagonal , chemistry , dehydrogenase , leucine , cube (algebra) , square (algebra) , enzyme , biology , biochemistry , geometry , physics , optics , bacteria , mathematics , genetics , amino acid , organic chemistry , gene , polymer
L‐Leucine dehydrogenase from Bacillus cereus was examined in the electron microscope. The quaternary structure reveals a molecule that is built up from 8 subunits, identical in mass, arranged in 2 layers which are oriented mainly in a staggered form. In each layer subunits are positioned at the vertices of a square, leaving free a central protein‐deficient region of 2.6 nm in diameter. The enzyme measures 11.1 nm in diagonal and 9.0 nm in edge length. Mean subunit diameter is 4.0 nm. The overall shape is a cube, slightly compressed, with 90% edge length in height.