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Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor
Author(s) -
Youn HyungSeop,
Lee JungGyu,
An Jun Yop,
Eom Soo Hyun
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb93
Subject(s) - antiparallel (mathematics) , ftsz , dimer , nucleoid , crystallography , cell division , topology (electrical circuits) , bacterial cell structure , domain (mathematical analysis) , biophysics , crystal structure , chemistry , escherichia coli , cell , biology , physics , bacteria , genetics , biochemistry , gene , mathematics , mathematical analysis , organic chemistry , quantum mechanics , combinatorics , magnetic field
In gram negative bacteria, proper placement of the FtsZ ring, mediated by nucleoid occlusion and the activities of the dynamic oscillating Min proteins MinC, MinD and MinE, is required for correct positioning of the cell division septum. MinE is a topological specificity factor that counters the activity of MinCD division inhibitor at the mid‐cell division site. Its structure consists of an anti‐MinCD domain and a topology specificity domain (TSD). Previous NMR analysis of truncated Escherichia coli MinE showed that the TSD domain contains a long α‐helix and two antiparallel β‐strands, which mediate formation of a homodimeric α/β structure. Here we present the crystal structure of full‐length Helicobacter pylori MinE and redefine its TSD based on that structure. The N‐terminal region of the TSD (residues 19–26), previously defined as part of the anti‐MinCD domain, forms a β‐strand (βA) and participates in TSD folding. In addition, H. pylori MinE forms a dimer through the interaction of anti‐parallel βA‐strands. Moreover, we observed serial dimer‐dimer interactions within the crystal packing, resulting in the formation of a filamentous structure. We therefore redefine the functional domain of MinE and propose that a multimeric filamentous structure is formed through anti‐parallel β‐strand interactions. This work was supported by the “Systems biology infrastructure establishment grant” provided by GIST.