2nd9

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nd9 OCA], [https://pdbe.org/2nd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nd9 RCSB], [https://www.ebi.ac.uk/pdbsum/2nd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nd9 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ.,Manuse S, Jean NL, Guinot M, Lavergne JP, Laguri C, Bougault CM, VanNieuwenhze MS, Grangeasse C, Simorre JP Nat Commun. 2016 Jun 27;7:12071. doi: 10.1038/ncomms12071. PMID:27346279<ref>PMID:27346279</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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