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. 2002 Oct;184(20):5753–5761. doi: 10.1128/JB.184.20.5753-5761.2002

FIG. 4.

FIG. 4.

Alignment of highly conserved sequences in glucansucrase catalytic domains. AS, N. polysaccharea (40); GTF-A, L. reuteri (59); GTF-B, Streptococcus mutans GS5 (51); GTF-I, S. downei Mfe28 (15); GTF-S, S. downei Mfe28 (18); DSR-S, L. mesenteroides NRRL B-512F (61); DSR-A, L. mesenteroides NRRL B-1299 (29); DSR-B, L. mesenteroides NRRL B-1299 (31); ASR, L. mesenteroides NRRL B-1355 (3); CD1 and CD2, catalytic domains of DSR-E, L. mesenteroides NRRL B-1299 (this study); —, gap in the sequence; ▪, key amino acid residues of the N-terminal end of the catalytic domain (35); ⇓, putative acid catalyst (9, 26); ➣ putative nucleophile (9, 26); •, putative calcium binding site (9); ⧫, putative residues stabilizing the transition state (26, 35); Δ, residue involved in glucan structure determination (34, 43, 49). Underlined sequences in italics are DSR-E sequences which diverge from consensus sequences.