view article
Figure 3
Multiple sequence alignment of MinC. Alignment was performed using the program ClustalX (Thompson et al., 2002BB37) and included MinC from Escherichia coli, Salmonella typhimurium, Klebsiella pneumoniae 342, Cronobacter sakazakii ATCC BAA-894, Erwinia tasmaniensis, Pectobacterium atrosepticum SCRI1043, Baumannia cicadellinicola, Enterobacter sp. 638 and Proteus mirabilis HI4320. A separate box was used for Thermotoga maritima, Thermotoga petrophila RKU-1, Thermotoga neapolitana DSM 4359, Thermotoga lettingae TMO, Bacillus subtilis and Thermosipho melanesiensis BI429. Residues involved in hydrophobic interactions in the central region of MinCNTD are marked with black dots. Residues that are important for maintaining the long twisted antiparallel β1–β1 interaction are shown in yellow boxes. Each domain is boxed in a different color. The β1 in EcoMinCNTD and β1–β2 strands in TmaMinCNTD are shown. The species from which the MinC structure was determined is shown in bold.

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 20| Part 6| October 2013| Pages 984-988
doi:10.1107/S0909049513022760
Follow J. Synchrotron Rad.
Sign up for e-alerts
E-alerts
Follow J. Synchrotron Rad. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS