Molecules and Cells

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Fig. 2.

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Fig. 2. Sequence alignments of StZapD with other ZapD proteins. Multi-alignment of E. coli (UniProtKB/Swiss-Prot accession number J7QWY2) against ZapD from S. typhimurium ZapD (Uni-ProtKB/Swiss-Prot accession number P67693), Salmonella choleraesuis (Uni-ProtKB/Swiss-Prot accession number Q57TB7), Shigella sonnei (Uni-ProtKB/Swiss-Prot accession number Q3Z5Q7), Shigella flexneri (Uni-ProtKB/Swiss-Prot accession number Q83MF4), Yersinia pestis (UniProtKB/Swiss-Prot accession number Q8ZBH9), Vibrio parahaemolyticus (UniProtKB/Swiss-Prot accession number Q87LT3), Vibrio vulnificus (UniProtKB/Swiss-Prot accession number P67695), Vibrio cholerae sero-type O1 (UniProtKB/Swiss-Prot accession number P67694), and Vibrio fischeri (UniProtKB/Swiss-Prot accession number Q5E2R1). Secondary structure elements were assigned by PyMOL (The PyMOL Molecular Graphics System, ) and every twentieth residue is marked by a black dot. Strictly (100%) and semi-conserved residues (80% and 60%) are highlighted in green, cyan, and yellow, respectively. Arrows and cylinders above the sequences denote α-helices and β-strands, respectively. Blue triangles indicate the mutation sites for EcZapD-EcFtsZ binding study.
Mol. Cells 2016;39:814~820 https://doi.org/10.14348/molcells.2016.0202
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