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Structural and mutational analysis of the cell division protein FtsQ
Author(s) -
Van Den Ent Fusinita,
Vinkenvleugel Thessa M. F.,
Ind Alice,
West Philip,
Veprintsev Dmitry,
Nanninga Nanne,
Den Blaauwen Tanneke,
Löwe Jan
Publication year - 2008
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06141.x
Subject(s) - periplasmic space , cell division , biology , cytokinesis , cell cycle protein , ftsz , microbiology and biotechnology , membrane protein , cytoplasm , escherichia coli , cell , genetics , cell cycle , gene , membrane
Summary Bacterial cytokinesis requires the divisome, a complex of proteins that co‐ordinates the invagination of the cytoplasmic membrane, inward growth of the peptidoglycan layer and the outer membrane. Assembly of the cell division proteins is tightly regulated and the order of appearance at the future division site is well organized. FtsQ is a highly conserved component of the divisome among bacteria that have a cell wall, where it plays a central role in the assembly of early and late cell division proteins. Here, we describe the crystal structure of the major, periplasmic domain of FtsQ from Escherichia coli and Yersinia enterocolitica . The crystal structure reveals two domains; the α‐domain has a striking similarity to polypeptide transport‐associated (POTRA) domains and the C‐terminal β‐domain forms an extended β‐sheet overlaid by two, slightly curved α‐helices. Mutagenesis experiments demonstrate that two functions of FtsQ, localization and recruitment, occur in two separate domains. Proteins that localize FtsQ need the second β‐strand of the POTRA domain and those that are recruited by FtsQ, like FtsL/FtsB, require the surface formed by the tip of the last α‐helix and the two C‐terminal β‐strands. Both domains act together to accomplish the role of FtsQ in linking upstream and downstream cell division proteins within the divisome.