2NDA
Solution structure of MapZ extracellular domain second subdomain
Summary for 2NDA
| Entry DOI | 10.2210/pdb2nda/pdb |
| Related | 2ND9 |
| NMR Information | BMRB: 26053 |
| Descriptor | Mid-cell-anchored protein Z (1 entity in total) |
| Functional Keywords | mapz, ftsz, peptidoglycan, division, cell cycle |
| Biological source | Streptococcus pneumoniae R6 (Streptococcus pneumoniae) |
| Cellular location | Cell membrane ; Single-pass membrane protein : Q8DR55 |
| Total number of polymer chains | 1 |
| Total formula weight | 12311.38 |
| Authors | Jean, N.L.,Manuse, S.,Guinot, M.,Bougault, C.M.,Grangeasse, C.,Simorre, J.-P. (deposition date: 2016-05-11, release date: 2016-06-29, Last modification date: 2024-05-01) |
| Primary citation | Manuse, S.,Jean, N.L.,Guinot, M.,Lavergne, J.P.,Laguri, C.,Bougault, C.M.,VanNieuwenhze, M.S.,Grangeasse, C.,Simorre, J.P. Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ. Nat Commun, 7:12071-12071, 2016 Cited by PubMed Abstract: 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. PubMed: 27346279DOI: 10.1038/ncomms12071 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
