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Crystal structure of apo‐glycolate oxidase
Author(s) -
Sandalova Tatyana,
Lindqvist Ylva
Publication year - 1993
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(93)81021-q
Subject(s) - chemistry , crystal structure , crystallography , cofactor , protein structure , enzyme , protein crystallization , resolution (logic) , stereochemistry , biochemistry , crystallization , organic chemistry , artificial intelligence , computer science
The crystal structure of the apoform of the α/β‐barrel enzyme glycolate oxidase has been determined to 2.6 Å resolution. Removal of the tightly bound cofactor FMN has a very strong influence on the protein structure; it is converted into a very flexible state, verging on a molten globule type of structure. The asymmetric unit contains two subunits with different conformations to each other and to the holo‐enzyme. The secondary structures are preserved, but their mutual arrangement has changed to some extent introducing cavities into the protein. The largest structural shifts are, however, found in the loops.