Open AccessSecondary structure of Streptococcus downei GTF‐I glucansucrase
Author(s) -
Monchois Vincent,
Lakey Jeremy H.,
Russell Roy R.B.
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13739.x
Subject(s) - leuconostoc mesenteroides , protein secondary structure , circular dichroism , protein structure , protein primary structure , sequence (biology) , biology , structure function , peptide sequence , crystallography , biochemistry , chemistry , genetics , bacteria , physics , lactic acid , particle physics , gene
Multiple sequence alignment and structure prediction of glucansucrases produced by oral streptococci and Leuconostoc mesenteroides showed that all have common structural features, with three major domains. There is no conservation of primary sequence or structure in the N‐terminal variable region. Sequence‐based structure prediction combined with circular dichroism spectrum analysis of purified truncated forms of Streptococcus downei GTF‐I revealed that the core catalytic region has a defined structure consistent with the proposed (α/β) 8 ‐barrel structure. The C‐terminal domain is a mixed structure with significant amounts of β‐sheet and random‐coil. This information contributes to the development of our understanding of structure‐function relationships in glucansucrases.