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Figure 2 | BMC Biotechnology

Figure 2

From: A new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) affects Soybean Asian rust (Phakopsora pachyrhizi) spore germination

Figure 2

Amino acid sequence alignment of selected GH18 plant members and secondary structure prediction. Conserved residues are marked with a shadow. Region encompassing the catalytic domain of class III chitinases are marked with a continuous box. In CaclXIP the catalytic residue of GH18 (marked with *), a Glutamic acid (E), is replaced by a Glutamine (Q), much as in Concanavalin B. On the other hand, in XIP-I the glutamic acid in the active site is conserved, even though it does not show any chitinolytic activity. Sequences in the doted box show residues involved in complexing with GH10 or GH11 xylanases in XIP-I and its counterparts in the other proteins. Secondary structure alignment was performed with Jalview software and improved by hand. The table of sequence identity was obtained with free on line software ClustalW2 (http://www.ebi.ac.uk/Tools/clustalw2). Sequences of Hevamine [GenBank:DQ873889], Concanavalin B [Swiss-Prot:P49347], and XIP-I [Swiss-Prot:Q8L5C6] were obtained at NCBI (http://www.ncbi.nlm.nih.gov) data bank.

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BMC Biotechnology

ISSN: 1472-6750

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