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PDBsum entry 2nd9
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References listed in PDB file
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Key reference
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Title
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Structure-Function analysis of the extracellular domain of the pneumococcal cell division site positioning protein mapz.
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Authors
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S.Manuse,
N.L.Jean,
M.Guinot,
J.P.Lavergne,
C.Laguri,
C.M.Bougault,
M.S.Vannieuwenhze,
C.Grangeasse,
J.P.Simorre.
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Ref.
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Nat Commun, 2016,
7,
12071.
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PubMed id
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Abstract
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Accurate placement of the bacterial division site is a prerequisite for the
generation of two viable and identical daughter cells. In Streptococcus
pneumoniae, the positive regulatory mechanism involving the membrane protein
MapZ positions precisely the conserved cell division protein FtsZ at the cell
centre. Here we characterize the structure of the extracellular domain of MapZ
and show that it displays a bi-modular structure composed of two subdomains
separated by a flexible serine-rich linker. We further demonstrate in vivo that
the N-terminal subdomain serves as a pedestal for the C-terminal subdomain,
which determines the ability of MapZ to mark the division site. The C-terminal
subdomain displays a patch of conserved amino acids and we show that this patch
defines a structural motif crucial for MapZ function. Altogether, this
structure-function analysis of MapZ provides the first molecular
characterization of a positive regulatory process of bacterial cell division.
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